2bzd

From Proteopedia

Revision as of 14:48, 30 October 2007

GALACTOSE RECOGNITION BY THE CARBOHYDRATE-BINDING MODULE OF A BACTERIAL SIALIDASE.

Overview

Glycoside hydrolases often possess carbohydrate-binding modules (CBMs) in, addition to their catalytic domains, which help target the enzymes to, appropriate substrates and thereby increase their catalytic efficiency., Sialidases hydrolyse the release of sialic acid from a variety of, glycoconjugates and play significant roles in the pathogenesis of a number, of important diseases. The sialidase from Micromonospora viridifaciens has, a CBM which recognizes galactose. The CBM is linked to the catalytic, domain by an immunoglobulin-like domain, resulting in the galactose, binding site sitting above the catalytic site, suggesting an interplay, between the two sites. By studying nine crystallographically independent, structures of the M. viridifaciens sialidase, the relative flexibility of, ... [(full description)]

About this Structure

2BZD is a [Single protein] structure of sequence from [Micromonospora viridifaciens] with GAL, NA and GOL as [ligands]. This structure superseeds the now removed PDB entry 2BQ9. Active as [Exo-alpha-sialidase], with EC number [3.2.1.18]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Galactose recognition by the carbohydrate-binding module of a bacterial sialidase., Newstead SL, Watson JN, Bennet AJ, Taylor G, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1483-91. Epub 2005, Oct 19. PMID:16239725

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