1kit: Difference between revisions

Revision as of 14:34, 21 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 Thu Feb 21 13:34:37 2008

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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 Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Vibrio cholerae]]
-[[Category: Crennell, S.J.]]
+[[Category: Crennell, S J.]]
-[[Category: Garman, E.F.]]
+[[Category: Garman, E F.]]
-[[Category: Laver, W.G.]]
+[[Category: Laver, W G.]]
-[[Category: Taylor, G.L.]]
+[[Category: Taylor, G L.]]
-[[Category: Vimr, E.R.]]
+[[Category: Vimr, E R.]]
 [[Category: CA]]
 [[Category: calcium]]
@@ Line 26: / Line 26: @@
 [[Category: signal]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:52:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:37 2008''