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Structure and Mechanism of DHHC Protein Acyltransferases.
Journal of Molecular Biology ( IF 5.6 ) Pub Date : 2020-06-06 , DOI: 10.1016/j.jmb.2020.05.023
Robyn Stix 1 , Chul-Jin Lee 2 , José D Faraldo-Gómez 1 , Anirban Banerjee 2
Affiliation  

S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands of proteins are targets of this post-translational modification, which is catalyzed by a family of eukaryotic integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs). Our knowledge of the repertoire of S-acylated proteins has been rapidly expanding owing to development of the chemoproteomic techniques. There has also been an increasing number of reports in the literature documenting the importance of S-acylation in human physiology and disease. Recently, the first atomic structures of two different DHHC-PATs were determined using X-ray crystallography. This review will focus on the insights gained into the molecular mechanism of DHHC-PATs from these structures and highlight representative data from the biochemical literature that they help explain.



中文翻译:

DHHC 蛋白酰基转移酶的结构和机制。

S-酰化,其中脂肪酸链通过硫酯键与半胱氨酸残基共价连接,是最普遍的蛋白质脂质修饰类型。数以千计的蛋白质是这种翻译后修饰的目标,它由称为 DHHC 蛋白酰基转移酶 (DHHC-PAT) 的真核整合膜酶家族催化。由于化学蛋白质组学技术的发展,我们对 S-酰化蛋白质库的了解迅速扩大。文献中也有越来越多的报告记录了 S-酰化在人体生理学和疾病中的重要性。最近,使用 X 射线晶体学确定了两种不同 DHHC-PAT 的第一个原子结构。

更新日期:2020-06-06
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