Crystal structure of the outer membrane protein OmpU from Vibrio cholerae at 2.2 A resolution.

ABSTRACT: Vibrio cholerae causes a severe disease that kills thousands of people annually. The outer membrane protein OmpU is the most abundant outer membrane protein in V. cholerae, and has been identified as an important virulence factor that is involved in host-cell interaction and recognition, as well as being critical for the survival of the pathogenic V. cholerae in the host body and in harsh environments. The mechanism of these processes is not well understood owing to a lack of the structure of V. cholerae OmpU. Here, the crystal structure of the V. cholerae OmpU trimer is reported to a resolution of 2.2 Å. The protomer forms a 16-β-stranded barrel with a noncanonical N-terminal coil located in the lumen of the barrel that consists of residues Gly32-Ser42 and is observed to participate in fo

SUBMITTER: Li H 

PROVIDER: S-EPMC5786005 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature