2v73: Difference between revisions
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Revision as of 18:39, 30 October 2007
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THE STRUCTURE OF THE FAMILY 40 CBM FROM C. PERFRINGENS NANJ IN COMPLEX WITH A SIALIC ACID CONTAINING MOLECULE
OverviewOverview
Myonecrotic isolates of Clostridium perfringens secrete multimodular, sialidases, often termed "large sialidases", that contribute to the, virulence of this bacterium. NanJ is the largest of the two secreted, sialidases at 1173 amino acids and comprises 6 different modules which, are, from the N-terminus, a family 32 carbohydrate binding module (CBM), a, family 40 CBM, a family 33 glycoside hydrolase, a module of unknown, function, a family 82 "X-module" of unknown function, and a module with, amino acid similarity to fibronectin type III domains. The hydrolase, activity of clostridial sialidases is quite well documented; however, the, functions of their accessory domains are entirely uninvestigated. Here we, describe the carbohydrate binding activity of the isolated family 32 CBM, ... [(full description)]
About this StructureAbout this Structure
2V73 is a [Single protein] structure of sequence from [Clostridium perfringens] with SIA and CA as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Carbohydrate Recognition by a Large Sialidase Toxin from Clostridium perfringens., Boraston AB, Ficko-Blean E, Healey M, Biochemistry. 2007 Oct 9;46(40):11352-60. Epub 2007 Sep 13. PMID:17850114
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