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Crystal structure of the outer membrane protein OmpU from Vibrio cholerae at 2.2 Å resolution
Author(s) -
Li Huanyu,
Zhang Weijiao,
Dong Changjiang
Publication year - 2018
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798317017697
Subject(s) - vibrio cholerae , bacterial outer membrane , biology , virulence , microbiology and biotechnology , biophysics , bacteria , biochemistry , genetics , escherichia coli , gene
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 forming the second gate in the pore. By mapping the published functional data onto the OmpU structure, the OmpU structure reinforces the notion that the long extracellular loop L4 with a β‐hairpin‐like motif may be critical for host‐cell binding and invasion, while L3, L4 and L8 are crucially implicated in phage recognition by V. cholerae .