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Structural coordination of polymerization and crosslinking by a SEDS-bPBP peptidoglycan synthase complex.
Nature Microbiology ( IF 28.3 ) Pub Date : 2020-03-09 , DOI: 10.1038/s41564-020-0687-z
Megan Sjodt 1 , Patricia D A Rohs 2 , Morgan S A Gilman 1 , Sarah C Erlandson 1 , Sanduo Zheng 1 , Anna G Green 3 , Kelly P Brock 3 , Atsushi Taguchi 2 , Daniel Kahne 4 , Suzanne Walker 2 , Debora S Marks 3 , David Z Rudner 2 , Thomas G Bernhardt 2, 5 , Andrew C Kruse 1
Affiliation  

The shape, elongation, division and sporulation (SEDS) proteins are a highly conserved family of transmembrane glycosyltransferases that work in concert with class B penicillin-binding proteins (bPBPs) to build the bacterial peptidoglycan cell wall1,2,3,4,5,6. How these proteins coordinate polymerization of new glycan strands with their crosslinking to the existing peptidoglycan meshwork is unclear. Here, we report the crystal structure of the prototypical SEDS protein RodA from Thermus thermophilus in complex with its cognate bPBP at 3.3 Å resolution. The structure reveals a 1:1 stoichiometric complex with two extensive interaction interfaces between the proteins: one in the membrane plane and the other at the extracytoplasmic surface. When in complex with a bPBP, RodA shows an approximately 10 Å shift of transmembrane helix 7 that exposes a large membrane-accessible cavity. Negative-stain electron microscopy reveals that the complex can adopt a variety of different conformations. These data define the bPBP pedestal domain as the key allosteric activator of RodA both in vitro and in vivo, explaining how a SEDS–bPBP complex can coordinate its dual enzymatic activities of peptidoglycan polymerization and crosslinking to build the cell wall.



中文翻译:

SEDS-bPBP肽聚糖合酶复合物的聚合和交联的结构协调。

形状,延伸,分裂和孢子形成(SEDS)蛋白是高度保守的跨膜糖基转移酶家族,可与B类青霉素结合蛋白(bPBP)协同作用,以构建细菌肽聚糖细胞壁1,2,3,4,5 ,6。这些蛋白质如何通过交联到现有的肽聚糖网状结构来协调新聚糖链的聚合反应尚不清楚。在这里,我们报告了Thermus thermophilus的原型SEDS蛋白RodA的晶体结构。与其3.3 b分辨率的同源bPBP配合使用。该结构揭示了一种1:1化学计量的复合物,在蛋白质之间具有两个广泛的相互作用界面:一个在膜平面中,另一个在胞质外表面。当与bPBP复合时,RodA会显示跨膜螺旋7位移约10,从而暴露出一个大的可触及膜腔。负染色电子显微镜显示该配合物可以采用多种不同的构象。这些数据将bPBP基座域定义为RodA在体外和体内的关键变构活化剂,从而说明SEDS-bPBP复合物如何协调其肽聚糖聚合和交联的双重酶促活性,从而建立细胞壁。

更新日期:2020-03-09
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