6PL6

Structural coordination of polymerization and crosslinking by a peptidoglycan synthase complex

6PL6 の概要

• エントリーDOI: 10.2210/pdb6pl6/pdb
• 関連するPDBエントリー: 6PL5
• 分子名称: Peptidoglycan glycosyltransferase RodA, Penicillin-binding protein 2/cell division protein FtsI, Unknown peptide, ... (4 entities in total)
• 機能のキーワード: peptidoglycan glycosyltransferase, transmembrane protein, shape elongation division and sporulation, elongasome, peptidoglycan transpeptidase, membrane protein
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 107311.51

構造登録者

Sjodt, M.,Rohs, P.D.A.,Erlandson, S.C.,Zheng, S.,Rudner, D.Z.,Bernhardt, T.G.,Kruse, A.C. (登録日: 2019-06-30, 公開日: 2020-03-18, 最終更新日: 2024-11-20)

主引用文献

Sjodt, M.,Rohs, P.D.A.,Gilman, M.S.A.,Erlandson, S.C.,Zheng, S.,Green, A.G.,Brock, K.P.,Taguchi, A.,Kahne, D.,Walker, S.,Marks, D.S.,Rudner, D.Z.,Bernhardt, T.G.,Kruse, A.C.
Structural coordination of polymerization and crosslinking by a SEDS-bPBP peptidoglycan synthase complex.
Nat Microbiol, 5:813-820, 2020

PubMed Abstract: 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. 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.

PubMed: 32152588
DOI: 10.1038/s41564-020-0687-z

実験手法

X-RAY DIFFRACTION (3.3 Å)