-
Discovery and characterization of a pan-betacoronavirus S2-binding antibody Structure (IF 4.4) Pub Date : 2024-09-25 Nicole V. Johnson, Steven C. Wall, Kevin J. Kramer, Clinton M. Holt, Sivakumar Periasamy, Simone I. Richardson, Nelia P. Manamela, Naveenchandra Suryadevara, Emanuele Andreano, Ida Paciello, Giulio Pierleoni, Giulia Piccini, Ying Huang, Pan Ge, James D. Allen, Naoko Uno, Andrea R. Shiakolas, Kelsey A. Pilewski, Rachel S. Nargi, Rachel E. Sutton, Ivelin S. Georgiev
-
Structural insights into translocation and tailored synthesis of hyaluronan Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-25 Ireneusz Górniak, Zachery Stephens, Satchal K. Erramilli, Tomasz Gawda, Anthony A. Kossiakoff, Jochen Zimmer
-
Advances in the field of RNA 3D structure prediction and modeling, with purely theoretical approaches, and with the use of experimental data Structure (IF 4.4) Pub Date : 2024-09-24 Sunandan Mukherjee, S. Naeim Moafinejad, Nagendar Goud Badepally, Katarzyna Merdas, Janusz M. Bujnicki
Recent advancements in RNA three-dimensional (3D) structure prediction have provided significant insights into RNA biology, highlighting the essential role of RNA in cellular functions and its therapeutic potential. This review summarizes the latest developments in computational methods, particularly the incorporation of artificial intelligence and machine learning, which have improved the efficiency
-
Improved higher resolution cryo-EM structures reveal the binding modes of hERG channel inhibitors Structure (IF 4.4) Pub Date : 2024-09-24 Yasuomi Miyashita, Toshio Moriya, Takafumi Kato, Masato Kawasaki, Satoshi Yasuda, Naruhiko Adachi, Kano Suzuki, Satoshi Ogasawara, Tetsuichiro Saito, Toshiya Senda, Takeshi Murata
-
An AI-informed NMR structure reveals an extraordinary LETM1 F-EF-hand domain that functions as a two-way regulator of mitochondrial calcium Structure (IF 4.4) Pub Date : 2024-09-23 Qi-Tong Lin, Danielle M. Colussi, Taylor Lake, Peter B. Stathopulos
-
Structural insights into CXCR4 modulation and oligomerization Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-23 Kei Saotome, Luke L. McGoldrick, Jo-Hao Ho, Trudy F. Ramlall, Sweta Shah, Michael J. Moore, Jee Hae Kim, Raymond Leidich, William C. Olson, Matthew C. Franklin
-
Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan Structure (IF 4.4) Pub Date : 2024-09-20 Michael J.M. Anderson, Amanda N. Hayward, Adam T. Smiley, Ke Shi, Matthew R. Pawlak, Eric J. Aird, Eva Grant, Lauren Greenberg, Hideki Aihara, Robert L. Evans, Christopher Ulens, Wendy R. Gordon
-
Super-silencer perturbation by EZH2 and REST inhibition leads to large loss of chromatin interactions and reduction in cancer growth Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-20 Ying Zhang, Kaijing Chen, Seng Chuan Tang, Yichao Cai, Akiko Nambu, Yi Xiang See, Chaoyu Fu, Anandhkumar Raju, Benjamin Lebeau, Zixun Ling, Jia Jia Chan, Yvonne Tay, Marek Mutwil, Manikandan Lakshmanan, Greg Tucker-Kellogg, Wee Joo Chng, Daniel G. Tenen, Motomi Osato, Vinay Tergaonkar, Melissa Jane Fullwood
-
Cryo-EM structures of the Spo11 core complex bound to DNA Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-20 You Yu, Juncheng Wang, Kaixian Liu, Zhi Zheng, Meret Arter, Corentin Claeys Bouuaert, Stephen Pu, Dinshaw J. Patel, Scott Keeney
-
Utilizing anomalous signals for element identification in macromolecular crystallography. Acta Cryst. D (IF 2.6) Pub Date : 2024-10-01 Kamel El Omari,Ismay Forsyth,Ramona Duman,Christian M Orr,Vitaliy Mykhaylyk,Erika J Mancini,Armin Wagner
AlphaFold2 has revolutionized structural biology by offering unparalleled accuracy in predicting protein structures. Traditional methods for determining protein structures, such as X-ray crystallography and cryo-electron microscopy, are often time-consuming and resource-intensive. AlphaFold2 provides models that are valuable for molecular replacement, aiding in model building and docking into electron
-
Folding of N-terminally acetylated α-synuclein upon interaction with lipid membranes. Biophys. J. (IF 3.2) Pub Date : 2024-09-20 Zihan Tang,Zhou Fang,Xuwei Wu,Jie Liu,Liangfei Tian,Xuejin Li,Jiajie Diao,Baohua Ji,Dechang Li
α-Synuclein (α-syn) is an abundant presynaptic neuronal protein whose aggregation is strongly associated with Parkinson's disease. It has been proposed that lipid membranes significantly affect the α-syn's aggregation process. Extensive studies have been conducted to understand the interactions between α-syn and lipid membranes and have demonstrated that the N-terminus plays a critical role. However
-
Unraveling the Dance of Phosphoproteins at Adhesion Planes: Modeling YAP Phosphorylation by a Particle-Based Stochastic Model. Biophys. J. (IF 3.2) Pub Date : 2024-09-20 Bo Cheng
-
The human touch: Utilizing AlphaFold 3 to analyze structures of endogenous metabolons Structure (IF 4.4) Pub Date : 2024-09-19 Toni K. Träger, Christian Tüting, Panagiotis L. Kastritis
-
Catalytic and noncatalytic functions of DNA polymerase κ in translesion DNA synthesis Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-19 Selene Sellés-Baiget, Sara M. Ambjørn, Alberto Carli, Ivo A. Hendriks, Irene Gallina, Norman E. Davey, Bente Benedict, Alessandra Zarantonello, Sampath A. Gadi, Bob Meeusen, Emil P. T. Hertz, Laura Slappendel, Daniel Semlow, Shana Sturla, Michael L. Nielsen, Jakob Nilsson, Thomas C. R. Miller, Julien P. Duxin
-
Publisher Correction: Structural basis of LRPPRC-SLIRP-dependent translation by the mitoribosome. Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-19 Vivek Singh,J Conor Moran,Yuzuru Itoh,Iliana C Soto,Flavia Fontanesi,Mary Couvillion,Martijn A Huynen,L Stirling Churchman,Antoni Barrientos,Alexey Amunts
-
Ligand-induced conformational changes in protein molecules detected by sum-frequency generation (SFG). Biophys. J. (IF 3.2) Pub Date : 2024-09-19 Joshua Salafsky,Patrik K Johansson,Elwy Abdelkader,Gottfried Otting
We present the first demonstration of ligand-induced conformational changes in a biological molecule, a protein, by sum-frequency generation (SFG). Constructs of KRasG12D protein were prepared by selectively deuterating residues of a single amino acid type using isotope-labeled amino acids and cell-free protein synthesis (CFPS). By attaching labeled protein to a supported bilayer membrane via a His-tag
-
Lys716 in the transmembrane domain of yeast mitofusin Fzo1 modulates anchoring and fusion Structure (IF 4.4) Pub Date : 2024-09-18 Raphaëlle Versini, Marc Baaden, Laetitia Cavellini, Mickaël M. Cohen, Antoine Taly, Patrick F.J. Fuchs
-
AlphaFold with conformational sampling reveals the structural landscape of homorepeats Structure (IF 4.4) Pub Date : 2024-09-18 David Fernandez Bonet, Shahrayar Ranyai, Luay Aswad, David P. Lane, Marie Arsenian-Henriksson, Michael Landreh, Dilraj Lama
-
The future of integrated structural biology Structure (IF 4.4) Pub Date : 2024-09-17 Harald Schwalbe, Pauline Audergon, Natalie Haley, Claudia Alen Amaro, Jon Agirre, Marc Baldus, Lucia Banci, Wolfgang Baumeister, Martin Blackledge, Jose Maria Carazo, Kristina Djinovic Carugo, Patrick Celie, Isabella Felli, Darren J. Hart, Thomas Hauß, Lari Lehtiö, Kresten Lindorff-Larsen, José Márquez, André Matagne, Roberta Pierattelli, Matthias Wilmanns
Instruct-ERIC, “the European Research Infrastructure Consortium for Structural biology research,” is a pan-European distributed research infrastructure making high-end technologies and methods in structural biology available to users. Here, we describe the current state-of-the-art of integrated structural biology and discuss potential future scientific developments as an impulse for the scientific
-
Structural characterization of the POTRA domains from A. baumannii reveals new conformations in BamA Structure (IF 4.4) Pub Date : 2024-09-17 Claire Overly Cottom, Robert Stephenson, Dante Ricci, Lixinhao Yang, James C. Gumbart, Nicholas Noinaj
-
Structural basis for translational control by the human 48S initiation complex Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-17 Valentyn Petrychenko, Sung-Hui Yi, David Liedtke, Bee-Zen Peng, Marina V. Rodnina, Niels Fischer
-
Lipid Redistribution due to a Cell-Cell Fusion Pore. Biophys. J. (IF 3.2) Pub Date : 2024-09-17 David William Allender,Michael Schick
We consider the redistribution of lipids comprising the plasma membranes during cell-cell fusion, particularly due to the presence of a fusion pore. Assuming the membranes are of constant thickness, we find that the mole fraction of cholesterol increases in the directly apposed exoplasmic leaflets, and is decreased in the cytoplasmic leaflets. The redistribution of the phospholipids is obtained as
-
Mixed-scale versus multiscale models of muscle contraction. Biophys. J. (IF 3.2) Pub Date : 2024-09-17 Josh E Baker
-
Understanding the regulation of protein synthesis under stress conditions Biophys. J. (IF 3.2) Pub Date : 2024-09-14 Inayat Ullah Irshad, Ajeet K. Sharma
Protein synthesis regulation primarily occurs at translation initiation, the first step of gene translation. However, the regulation of translation initiation under various conditions is not fully understood. Specifically, the reason why protein production from certain mRNAs remains resistant to stress while others do not show such resilience. Moreover, why is protein production enhanced from a few
-
Free-energy transduction mechanisms shape the flux space of metabolic networks Biophys. J. (IF 3.2) Pub Date : 2024-09-14 Benjamin Pfeuty
The transduction of free energy in metabolic networks represents a thermodynamic mechanism by which the free energy derived from nutrients is converted to drive nonspontaneous, energy-requiring metabolic reactions. This transduction is typically observed in processes that generate energy-rich molecules such as ATP and NAD(P)H, which, in turn, power specific reactions, particularly biosynthetic reactions
-
Rewiring protein binding specificity in paralogous DRG/DFRP complexes Structure (IF 4.4) Pub Date : 2024-09-13 Christian A.E. Westrip, Stephen J. Smerdon, Mathew L. Coleman
-
Dynamics-based protein network features accurately discriminate neutral and rheostat positions Biophys. J. (IF 3.2) Pub Date : 2024-09-13 P. Campitelli, D. Ross, L. Swint-Kruse, S.B. Ozkan
In some proteins, a unique class of nonconserved positions is characterized by their ability to generate diverse functional outcomes through single amino acid substitutions. Due to their ability to tune protein function, accurately identifying such “rheostat” positions is crucial for protein design, for understanding the impact of mutations observed in humans, and for predicting the evolution of pathogen
-
Structural organization of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina acetivorans Structure (IF 4.4) Pub Date : 2024-09-11 Matteo Cossu, Daniel Catlin, Sean J. Elliott, William W. Metcalf, Satish K. Nair
-
Theoretical insights into rotary mechanism of MotAB in the bacterial flagellar motor Biophys. J. (IF 3.2) Pub Date : 2024-09-11 Shintaroh Kubo, Yasushi Okada, Shoji Takada
Many bacteria enable locomotion by rotating their flagellum. It has been suggested that this rotation is realized by the rotary motion of the stator unit, MotAB, which is driven by proton transfer across the membrane. Recent cryo-electron microscopy studies have revealed a 5:2 MotAB configuration, in which a MotB dimer is encircled by a ring-shaped MotA pentamer. Although the structure implicates the
-
Unraveling the hydration dynamics of the ACC1–13K24-ATP system: From liquid to droplet to amyloid fibril Biophys. J. (IF 3.2) Pub Date : 2024-09-11 Sampad Bag, Robert Dec, Simone Pezzotti, Rudhi Ranjan Sahoo, Gerhard Schwaab, Roland Winter, Martina Havenith
In order to achieve a comprehensive understanding of protein aggregation processes, an exploration of solvation dynamics, a key yet intricate component of biological phenomena, is mandatory. In the present study, we used Fourier transform infrared spectroscopy and terahertz spectroscopy complemented by atomic force microscopy and kinetic experiments utilizing thioflavin T fluorescence to elucidate
-
Dynamic formation of the protein-lipid prefusion complex Biophys. J. (IF 3.2) Pub Date : 2024-09-10 Maria Bykhovskaia
Synaptic vesicles (SVs) fuse with the presynaptic membrane (PM) to release neuronal transmitters. The SV protein synaptotagmin 1 (Syt1) serves as a Ca2+ sensor for evoked fusion. Syt1 is thought to trigger fusion by penetrating the PM upon Ca2+ binding; however, the mechanistic detail of this process is still debated. Syt1 interacts with the SNARE (soluble N-ethylmaleimide-sensitive factor attachment
-
Blocking uncertain mispriming errors of PCR Biophys. J. (IF 3.2) Pub Date : 2024-09-10 Takumi Takahashi, Hiroyuki Aoyanagi, Simone Pigolotti, Shoichi Toyabe
The polymerase chain reaction (PCR) plays a central role in genetic engineering and is routinely used in various applications, from biological and medical research to the diagnosis of viral infections. PCR is an extremely sensitive method for detecting target DNA sequences, but it is substantially error prone. In particular, the mishybridization of primers to contaminating sequences can result in false
-
Resistance of estrogen receptor function to BET bromodomain inhibition is mediated by transcriptional coactivator cooperativity Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-09 Sicong Zhang, Robert G. Roeder
-
Author Correction: Unwinding of a eukaryotic origin of replication visualized by cryo-EM. Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-09 Sarah S Henrikus,Marta H Gross,Oliver Willhoft,Thomas Pühringer,Jacob S Lewis,Allison W McClure,Julia F Greiwe,Giacomo Palm,Andrea Nans,John F X Diffley,Alessandro Costa
-
Exocyst stimulates multiple steps of exocytic SNARE complex assembly and vesicle fusion Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-06 Chanwoo Lee, Dante Lepore, Seung-Hak Lee, Tae Gyun Kim, Natasha Buwa, Jongchan Lee, Mary Munson, Tae-Young Yoon
-
Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-06 Martin Obr, Mathias Percipalle, Darya Chernikova, Huixin Yang, Andreas Thader, Gergely Pinke, Dario Porley, Louis M. Mansky, Robert A. Dick, Florian K. M. Schur
-
Pseudouridine guides germline small RNA transport and epigenetic inheritance Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-06 Rowan P. Herridge, Jakub Dolata, Valentina Migliori, Cristiane de Santis Alves, Filipe Borges, Andrea J. Schorn, Frédéric van Ex, Ann Lin, Mateusz Bajczyk, Jean-Sebastien Parent, Tommaso Leonardi, Alan Hendrick, Tony Kouzarides, Robert A. Martienssen
-
Driving forces of proton-pumping rhodopsins Biophys. J. (IF 3.2) Pub Date : 2024-09-06 Akari Okuyama, Shoko Hososhima, Hideki Kandori, Satoshi P. Tsunoda
Proton-pumping rhodopsins are light-driven proton transporters that have been discovered from various microbiota. They are categorized into two groups: outward-directed and inward-directed proton pumps. Although the directions of transport are opposite, they are active proton transporters that create an H+ gradient across a membrane. Here, we aimed to study the driving force of the proton-pumping rhodopsins
-
Cracking under stress: How actin might turn failure into action Biophys. J. (IF 3.2) Pub Date : 2024-09-06 Ulrich S. Schwarz
-
Neural control and innate self-tuning of the hair cell’s active process Biophys. J. (IF 3.2) Pub Date : 2024-09-06 Charles Metzler-Winslow, Martín A. Toderi, Dolores Bozovic
We propose a model for the feedback control processes that underlie the robustness and high sensitivity of mechanosensory hair cells. Our model encompasses self-tuning active processes intrinsic to these cells, which drive the amplification of mechanical stimuli by consuming metabolic energy, and a neural input process that protects these cells from damage caused by powerful stimuli. We explore the
-
RNA dynamics from experimental and computational approaches Structure (IF 4.4) Pub Date : 2024-09-05 Giovanni Bussi, Massimiliano Bonomi, Paraskevi Gkeka, Michael Sattler, Hashim M. Al-Hashimi, Pascal Auffinger, Maria Duca, Yann Foricher, Danny Incarnato, Alisha N. Jones, Serdal Kirmizialtin, Miroslav Krepl, Modesto Orozco, Giulia Palermo, Samuela Pasquali, Loïc Salmon, Harald Schwalbe, Eric Westhof, Martin Zacharias
Conformational dynamics is crucial for the biological function of RNA molecules and for their potential as therapeutic targets. This meeting report outlines key “take-home” messages that emerged from the presentations and discussions during the CECAM workshop “RNA dynamics from experimental and computational approaches” in Paris, June 26–28, 2023.
-
Ordering the disordered Structure (IF 4.4) Pub Date : 2024-09-05 Sarah Shammas, Gabriella Heller, Alaji Bah, Emmanouela Filippidi, Alex Holehouse, Miao Yu, Janin Lautenschläger
-
Expanding the insect defensin landscape Structure (IF 4.4) Pub Date : 2024-09-05 Krishnakoli Adhikary, Sébastien F. Poget
In this issue of Structure, Walker et al.1 determined the NMR structure of a recently discovered defensin, Pp19, from the venom of an assassin bug. This peptide adopts an α-defensin-like structure, which had not been observed in insects before. Unlike mammalian α-defensins, which are generally antimicrobial, Pp19 has insecticidal activity.
-
Ping, pong, and freeze: Structural insights into the inhibition of ceramide synthase by Fumonisin B1 Structure (IF 4.4) Pub Date : 2024-09-05 Kexin Hu, Yu Cao
Fumonisin B1 (FB1) targets sphingolipid biosynthesis, inhibiting ceramide synthases. In this issue of Structure, Zhang et al.1 determined the cryoelectron microscopic structures of yeast ceramide synthase in complex with FB1 and its acylated derivative, acyl-FB1, revealing a two-step “ping-pong” mechanism for the N-acylation of FB1 and how it inhibits ceramide synthase.
-
Antiterminator LoaP loads onto RNA to chase a runaway RNA polymerase Structure (IF 4.4) Pub Date : 2024-09-05 Bing Wang, Irina Artsimovitch
In this issue of Structure, Elghondakly et al.1 present the crystal structure of Thermoanaerobacter pseudethanolicus antiterminator LoaP, a member of a ubiquitous family of NusG transcription factors, bound to its target, a dfn RNA hairpin. LoaP uses RNA as a recognition determinant, which is unique among NusG paralogs and makes unusual contacts in the major groove of the RNA.
-
Structural review of SARS-CoV-2 antiviral targets Structure (IF 4.4) Pub Date : 2024-09-05 Wen Cui, Yinkai Duan, Yan Gao, Wei Wang, Haitao Yang
The coronavirus disease 2019 (COVID-19), the disease caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), represents the most disastrous infectious disease pandemic of the past century. As a member of the Betacoronavirus genus, the SARS-CoV-2 genome encodes a total of 29 proteins. The spike protein, RNA-dependent RNA polymerase, and proteases play crucial roles in the virus replication
-
Microcrystal electron diffraction structure of Toll-like receptor 2 TIR-domain-nucleated MyD88 TIR-domain higher-order assembly. Acta Cryst. D (IF 2.6) Pub Date : 2024-09-04 Y Li,L C Pacoste,W Gu,S J Thygesen,K J Stacey,T Ve,B Kobe,H Xu,J D Nanson
Eukaryotic TIR (Toll/interleukin-1 receptor protein) domains signal via TIR-TIR interactions, either by self-association or by interaction with other TIR domains. In mammals, TIR domains are found in Toll-like receptors (TLRs) and cytoplasmic adaptor proteins involved in pro-inflammatory signaling. Previous work revealed that the MAL TIR domain (MALTIR) nucleates the assembly of MyD88TIR into crystalline
-
Structural and functional mechanisms of anti-NMDAR autoimmune encephalitis Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-03 Kevin Michalski, Taha Abdulla, Sam Kleeman, Lars Schmidl, Ricardo Gómez, Noriko Simorowski, Francesca Vallese, Harald Prüss, Manfred Heckmann, Christian Geis, Hiro Furukawa
-
Shieldin and CST co-orchestrate DNA polymerase-dependent tailed-end joining reactions independently of 53BP1-governed repair pathway choice Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-03 Ashleigh King, Pia I. Reichl, Jean S. Metson, Robert Parker, Daniella Munro, Catarina Oliveira, Lucia Sommerova, Jordan R. Becker, Daniel Biggs, Chris Preece, Benjamin Davies, J. Ross Chapman
-
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-03 Han Wang, Chun Xie, Bo Deng, Jingjun Ding, Na Li, Zengwei Kou, Mengmeng Jin, Jie He, Qinrui Wang, Han Wen, Jinbao Zhang, Qinming Zhou, Sheng Chen, Xiangjun Chen, Ti-Fei Yuan, Shujia Zhu
-
Deep learning permits imaging of multiple structures with the same fluorophores Biophys. J. (IF 3.2) Pub Date : 2024-09-03 Luhong Jin, Jingfang Liu, Heng Zhang, Yunqi Zhu, Haixu Yang, Jianhang Wang, Luhao Zhang, Cuifang Kuang, Baohua Ji, Ju Zhang, Xu Liu, Yingke Xu
Fluorescence microscopy, which employs fluorescent tags to label and observe cellular structures and their dynamics, is a powerful tool for life sciences. However, due to the spectral overlap between different dyes, a limited number of structures can be separately labeled and imaged for live-cell applications. In addition, the conventional sequential channel imaging procedure is quite time consuming
-
YAP phosphorylation within integrin adhesions: Insights from a computational model Biophys. J. (IF 3.2) Pub Date : 2024-09-03 Hamidreza Jafarinia, Lidan Shi, Haguy Wolfenson, Aurélie Carlier
Mechanical and biochemical cues intricately activate Yes-associated protein (YAP), which is pivotal for the cellular responses to these stimuli. Recent findings reveal an unexplored role of YAP in influencing the apoptotic process. It has been shown that, on soft matrices, YAP is recruited to small adhesions, phosphorylated at Y357, and translocated into the nucleus triggering apoptosis. Interestingly
-
Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase Nat. Struct. Mol. Biol. (IF 12.5) Pub Date : 2024-09-02 Jiayue Su, Xuyang Tian, Hang Cheng, Desheng Liu, Ziyi Wang, Shan Sun, Hong-Wei Wang, Sen-Fang Sui
-
Microfluidic measurement of the size and shape of lipid-anchored proteins Biophys. J. (IF 3.2) Pub Date : 2024-09-02 Sreeja Sasidharan, Leah Knepper, Emily Ankrom, Gabriel Cucé, Lingyang Kong, Amanda Ratajczak, Wonpil Im, Damien Thévenin, Aurelia Honerkamp-Smith
The surface of a cell is crowded with membrane proteins. The size, shape, density, and mobility of extracellular surface proteins mediate cell surface accessibility to external molecules, viral particles, and other cells. However, predicting these qualities is not always straightforward, even when protein structures are known. We previously developed an experimental method for measuring flow-driven
-
Comparison of two crystal polymorphs of NowGFP reveals a new conformational state trapped by crystal packing. Acta Cryst. D (IF 2.6) Pub Date : 2024-09-02 Jin Kyun Kim,Hannah Jeong,Jeongwoo Seo,Seoyoon Kim,Kyung Hyun Kim,Duyoung Min,Chae Un Kim
Crystal polymorphism serves as a strategy to study the conformational flexibility of proteins. However, the relationship between protein crystal packing and protein conformation often remains elusive. In this study, two distinct crystal forms of a green fluorescent protein variant, NowGFP, are compared: a previously identified monoclinic form (space group C2) and a newly discovered orthorhombic form
-
Post-translational modifications in the Protein Data Bank. Acta Cryst. D (IF 2.6) Pub Date : 2024-08-29 Lucy C Schofield,Jordan S Dialpuri,Garib N Murshudov,Jon Agirre
Proteins frequently undergo covalent modification at the post-translational level, which involves the covalent attachment of chemical groups onto amino acids. This can entail the singular or multiple addition of small groups, such as phosphorylation; long-chain modifications, such as glycosylation; small proteins, such as ubiquitination; as well as the interconversion of chemical groups, such as the
-
Structural analysis of a ligand-triggered intermolecular disulfide switch in a major latex protein from opium poppy. Acta Cryst. D (IF 2.6) Pub Date : 2024-08-29 Samuel C Carr,Peter J Facchini,Kenneth K S Ng
Several proteins from plant pathogenesis-related family 10 (PR10) are highly abundant in the latex of opium poppy and have recently been shown to play diverse and important roles in the biosynthesis of benzylisoquinoline alkaloids (BIAs). The recent determination of the first crystal structures of PR10-10 showed how large conformational changes in a surface loop and adjacent β-strand are coupled to
-
Surface-mutagenesis strategies to enable structural biology crystallization platforms. Acta Cryst. D (IF 2.6) Pub Date : 2024-08-29 Martina Schaefer,Vera Pütter,André Hilpmann,Ursula Egner,Simon James Holton,Roman Christian Hillig
A key prerequisite for the successful application of protein crystallography in drug discovery is to establish a robust crystallization system for a new drug-target protein fast enough to deliver crystal structures when the first inhibitors have been identified in the hit-finding campaign or, at the latest, in the subsequent hit-to-lead process. The first crucial step towards generating well folded
-
Ras signaling mechanisms: New insights from single-molecule biophysics Biophys. J. (IF 3.2) Pub Date : 2024-08-31 Anne Marie McCombs, Joy R. Armendariz, Joseph J. Falke
-
Structural insights into the convergent evolution of sulfoxide synthase EgtB-IV, an ergothioneine-biosynthetic homolog of ovothiol synthase OvoA Structure (IF 4.4) Pub Date : 2024-08-30 Kendra A. Ireland, Chase M. Kayrouz, Marissa L. Abbott, Mohammad R. Seyedsayamdost, Katherine M. Davis