1kit
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VIBRIO CHOLERAE NEURAMINIDASE
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, ... [(full description)]
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]. Structure known Active Site: ACT. 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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