6VAT

Structure of the periplasmic domain of YejM from Salmonella typhimurium

Summary for 6VAT

• Entry DOI: 10.2210/pdb6vat/pdb
• Descriptor: Periplasmic domain of the cardiolipin transporter protein YejM/PbgA, TETRAETHYLENE GLYCOL, ETHANOLAMINE, ... (10 entities in total)
• Functional Keywords: yejm, membrane protein, hydrolase, phosphatase, cardiolipin, transport protein
• Biological source: Salmonella enterica subsp. enterica serovar
• Total number of polymer chains: 6
• Total formula weight: 250831.72

Authors

Gabale, U.,Ressl, S. (deposition date: 2019-12-17, release date: 2020-08-26, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.35 Å)