期刊
NATURE MICROBIOLOGY
卷 5, 期 6, 页码 813-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41564-020-0687-z
关键词
-
类别
资金
- National Institutes of Health [U19AI109764, R01GM106303, 5F31GM128233-02]
- Howard Hughes Medical Institute
- Canadian Institutes of Health Research
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 wall(1-6). 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 angstrom 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 angstrom 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. The crystal structure of the RodA-PBP2 complex from Thermus thermophilus elucidates how binding between these two proteins regulates their abilities to polymerize and crosslink peptidoglycan during bacterial cell wall synthesis.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据