1kit

OverviewOverview

BACKGROUND: Vibrio cholerae neuraminidase is part of a mucinase complex, which may function in pathogenesis by degrading the mucin layer of the, gastrointestinal tract. The neuraminidase, which has been the target of, extensive inhibitor studies, plays a subtle role in the pathology of the, bacterium, by processing higher order gangliosides to GM1, the receptor, for cholera toxin. RESULTS: We report here the X-ray crystal structure of, V. cholerae neuraminidase at 2.3 A resolution. The 83 kDa enzyme folds, into three distinct domains. The central catalytic domain has the, canonical neuraminidase beta-propeller fold, and is flanked by two domains, which possess identical legume lectin-like topologies but without the, usual metal-binding loops. The active site has many features in common, with other viral and bacterial neuraminidases but, uniquely, has an, essential Ca2+ ion which plays a crucial structural role. CONCLUSIONS: The, environment of the small intestine requires V. cholerae to secrete several, adhesins, and it is known that its neuraminidase can bind to cell, surfaces, and remain active. The unexpected lectin-like domains possibly, mediate this attachment. These bacterial lectin folds represent additional, members of a growing lectin superfamily.

About this StructureAbout this Structure

1KIT is a Single protein structure of sequence from Vibrio cholerae with CA as ligand. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain., Crennell S, Garman E, Laver G, Vimr E, Taylor G, Structure. 1994 Jun 15;2(6):535-44. PMID:7922030

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