1kit: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1kit.gif|left|200px]]<br /><applet load="1kit" size=" | [[Image:1kit.gif|left|200px]]<br /><applet load="1kit" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1kit, resolution 2.3Å" /> | caption="1kit, resolution 2.3Å" /> | ||
'''VIBRIO CHOLERAE NEURAMINIDASE'''<br /> | '''VIBRIO CHOLERAE NEURAMINIDASE'''<br /> | ||
| Line 7: | Line 7: | ||
==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/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] Known structural/functional Site: <scene name='pdbsite=ACT:Active Site'>ACT</scene>. Full crystallographic information is available from [http:// | 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 <scene name='pdbligand=CA:'>CA</scene> 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] Known structural/functional Site: <scene name='pdbsite=ACT:Active+Site'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIT OCA]. | ||
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: signal]] | [[Category: signal]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:52:51 2008'' | ||
Revision as of 10:52, 3 February 2008
|
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 with 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
Page seeded by OCA on Sun Feb 3 09:52:51 2008