7T6D

CryoEM structure of the YejM/LapB complex

7T6D の概要

• エントリーDOI: 10.2210/pdb7t6d/pdb
• EMDBエントリー: 25713
• 分子名称: Lipopolysaccharide assembly protein B, Inner membrane protein YejM, 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE, ... (4 entities in total)
• 機能のキーワード: yejm, ycim, regulation, lipopolysaccharide synthesis, lpxc, membrane protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 227221.16

構造登録者

Mi, W.,Shu, S. (登録日: 2021-12-13, 公開日: 2022-08-17, 最終更新日: 2024-02-28)

主引用文献

Shu, S.,Mi, W.
Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli.
Nat Commun, 13:4576-4576, 2022

PubMed Abstract: Lipopolysaccharide (LPS) is an essential glycolipid and forms a protective permeability barrier for most Gram-negative bacteria. In E. coli, LPS levels are under feedback control, achieved by FtsH-mediated degradation of LpxC, which catalyzes the first committed step in LPS synthesis. FtsH is a membrane-bound AAA+ protease, and its protease activity toward LpxC is regulated by essential membrane proteins LapB and YejM. However, the regulatory mechanisms are elusive. We establish an in vitro assay to analyze the kinetics of LpxC degradation and demonstrate that LapB is an adaptor protein that utilizes its transmembrane helix to interact with FtsH and its cytoplasmic domains to recruit LpxC. Our YejM/LapB complex structure reveals that YejM is an anti-adaptor protein, competing with FtsH for LapB to inhibit LpxC degradation. Structural analysis unravels that LapB and LPS have overlapping binding sites in YejM. Thus, LPS levels control formation of the YejM/LapB complex to determine LpxC protein levels.

PubMed: 35931690
DOI: 10.1038/s41467-022-32277-1

実験手法

ELECTRON MICROSCOPY (3.9 Å)