Ontology highlight
ABSTRACT:
SUBMITTER: Prince SM
PROVIDER: S-EPMC122538 | biostudies-literature | 2002 Mar
REPOSITORIES: biostudies-literature
Prince Stephen M SM Achtman Mark M Derrick Jeremy P JP
Proceedings of the National Academy of Sciences of the United States of America 20020312 6
OpcA is an integral outer membrane protein from Neisseria meningitidis, the causative agent of meningococcal meningitis and septicemia. It mediates the adhesion of N. meningitidis to epithelial and endothelial cells by binding to vitronectin and proteoglycan cell-surface receptors. Here, we report the determination of the crystal structure of OpcA to 2.0 A resolution. OpcA adopts a 10-stranded beta-barrel structure with extensive loop regions that protrude above the predicted surface of the memb ...[more]