6TPI

EnvC bound to the FtsX periplasmic domain

6TPI の概要

• エントリーDOI: 10.2210/pdb6tpi/pdb
• 分子名称: Murein hydrolase activator EnvC, Cell division protein FtsX (3 entities in total)
• 機能のキーワード: complex, protein binding
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 67642.52

構造登録者

Crow, A. (登録日: 2019-12-13, 公開日: 2020-11-04, 最終更新日: 2024-01-24)

主引用文献

Cook, J.,Baverstock, T.C.,McAndrew, M.B.L.,Stansfeld, P.J.,Roper, D.I.,Crow, A.
Insights into bacterial cell division from a structure of EnvC bound to the FtsX periplasmic domain.
Proc.Natl.Acad.Sci.USA, 117:28355-28365, 2020

PubMed Abstract: FtsEX is a bacterial ABC transporter that regulates the activity of periplasmic peptidoglycan amidases via its interaction with the murein hydrolase activator, EnvC. In , FtsEX is required to separate daughter cells after cell division and for viability in low-osmolarity media. Both the ATPase activity of FtsEX and its periplasmic interaction with EnvC are required for amidase activation, but the process itself is poorly understood. Here we present the 2.1 Å structure of the FtsX periplasmic domain in complex with its periplasmic partner, EnvC. The EnvC-FtsX periplasmic domain complex has a 1-to-2 stoichiometry with two distinct FtsX-binding sites located within an antiparallel coiled coil domain of EnvC. Residues involved in amidase activation map to a previously identified groove in the EnvC LytM domain that is here found to be occluded by a "restraining arm" suggesting a self-inhibition mechanism. Mutational analysis, combined with bacterial two-hybrid screens and in vivo functional assays, verifies the FtsEX residues required for EnvC binding and experimentally test a proposed mechanism for amidase activation. We also define a predicted link between FtsEX and integrity of the outer membrane. Both the ATPase activity of FtsEX and its periplasmic interaction with EnvC are required for resistance to membrane-attacking antibiotics and detergents to which would usually be considered intrinsically resistant. These structural and functional data provide compelling mechanistic insight into FtsEX-mediated regulation of EnvC and its downstream control of periplasmic peptidoglycan amidases.

PubMed: 33097670
DOI: 10.1073/pnas.2017134117

実験手法

X-RAY DIFFRACTION (2.1 Å)