6VDF

Structure of the periplasmic domain of YejM from Salmonella typhimurium (twinned)

6VDF の概要

• エントリーDOI: 10.2210/pdb6vdf/pdb
• 関連するPDBエントリー: 6VAT 6VC7
• 分子名称: Periplasmic domain of the cardiolipin transporter protein YejM/PbgA, TRIETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (8 entities in total)
• 機能のキーワード: yejm, membrane protein, hydrolase, phosphatase, cardiolipin, transport protein
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 165816.62

構造登録者

Gabale, U.,Ressl, S. (登録日: 2019-12-25, 公開日: 2020-08-26, 最終更新日: 2023-10-11)

主引用文献

Gabale, U.,Pena Palomino, P.A.,Kim, H.,Chen, W.,Ressl, S.
The essential inner membrane protein YejM is a metalloenzyme.
Sci Rep, 10:17794-17794, 2020

PubMed Abstract: Recent recurrent outbreaks of Gram-negative bacteria show the critical need to target essential bacterial mechanisms to fight the increase of antibiotic resistance. Pathogenic Gram-negative bacteria have developed several strategies to protect themselves against the host immune response and antibiotics. One such strategy is to remodel the outer membrane where several genes are involved. yejM was discovered as an essential gene in E. coli and S. typhimurium that plays a critical role in their virulence by changing the outer membrane permeability. How the inner membrane protein YejM with its periplasmic domain changes membrane properties remains unknown. Despite overwhelming structural similarity between the periplasmic domains of two YejM homologues with hydrolases like arylsulfatases, no enzymatic activity has been previously reported for YejM. Our studies reveal an intact active site with bound metal ions in the structure of YejM periplasmic domain. Furthermore, we show that YejM has a phosphatase activity that is dependent on the presence of magnesium ions and is linked to its function of regulating outer membrane properties. Understanding the molecular mechanism by which YejM is involved in outer membrane remodeling will help to identify a new drug target in the fight against the increased antibiotic resistance.

PubMed: 33082366
DOI: 10.1038/s41598-020-73660-6

実験手法

X-RAY DIFFRACTION (1.92 Å)