2bzd: Difference between revisions

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, the three domains was analysed. A detailed study is also presented of the, recognition of galactose and lactose by the M. viridifaciens CBM. The, striking structure of this sialidase suggests a role for the CBM in, binding to galactose residues unmasked by the adjacent catalytic site.

2BZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Micromonospora_viridifaciens Micromonospora viridifaciens] with GAL, NA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2BQ9. 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: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BZD OCA].  

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