1kit: Difference between revisions
New page: left|200px<br /> <applet load="1kit" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kit, resolution 2.3Å" /> '''VIBRIO CHOLERAE NEUR... |
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==About this Structure== | ==About this Structure== | ||
1KIT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KIT OCA]]. | 1KIT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7922030 7922030] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7922030 7922030] | ||
[[Category: Exo-alpha-sialidase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
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Revision as of 12:32, 30 October 2007
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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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