1kit: Difference between revisions
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[[Image:1kit.gif|left|200px]] | [[Image:1kit.gif|left|200px]] | ||
'''VIBRIO CHOLERAE NEURAMINIDASE''' | {{Structure | ||
|PDB= 1kit |SIZE=350|CAPTION= <scene name='initialview01'>1kit</scene>, resolution 2.3Å | |||
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] | |||
|GENE= NANH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae]) | |||
}} | |||
'''VIBRIO CHOLERAE NEURAMINIDASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KIT is a [ | 1KIT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIT OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7922030 7922030] | ||
[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:18:01 2008'' | ||
Revision as of 13:18, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Gene: | NANH (Vibrio cholerae) | ||||||
| Activity: | Exo-alpha-sialidase, with EC number 3.2.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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. 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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