1KIT
VIBRIO CHOLERAE NEURAMINIDASE
Summary for 1KIT
Entry DOI | 10.2210/pdb1kit/pdb |
Descriptor | SIALIDASE, CALCIUM ION (3 entities in total) |
Functional Keywords | hydrolase, glycosidase, calcium |
Biological source | Vibrio cholerae |
Cellular location | Secreted: P37060 |
Total number of polymer chains | 1 |
Total formula weight | 83119.63 |
Authors | Taylor, G.L.,Crennell, S.J.,Garman, E.F.,Vimr, E.R.,Laver, W.G. (deposition date: 1996-06-21, release date: 1997-06-05, Last modification date: 2024-02-14) |
Primary citation | Crennell, S.,Garman, E.,Laver, G.,Vimr, E.,Taylor, G. Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure, 2:535-544, 1994 Cited by PubMed Abstract: 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. PubMed: 7922030DOI: 10.1016/S0969-2126(00)00053-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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