Structural analysis of a Vibrio phospholipase reveals an unusual Ser-His-chloride catalytic triad.

ABSTRACT: Phospholipases can disrupt host membranes and are important virulence factors in many pathogens. VvPlpA is a phospholipase A₂ secreted by Vibrio vulnificus and essential for virulence. Its homologs, termed thermolabile hemolysins (TLHs), are widely distributed in Vibrio bacteria, but no structural information for this virulence factor class is available. Herein, we report the crystal structure of VvPlpA to 1.4-Å resolution, revealing that VvPlpA contains an N-terminal domain of unknown function and a C-terminal phospholipase domain and that these two domains are packed closely together. The phospholipase domain adopts a typical SGNH hydrolase fold, containing the four conserved catalytic residues Ser, Gly, Asn, and His. Interestingly, the struc

SUBMITTER: Wan Y 

PROVIDER: S-EPMC6663882 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature