2BZD

Galactose recognition by the carbohydrate-binding module of a bacterial sialidase.

Replaces:  2BQ9

Summary for 2BZD

• Entry DOI: 10.2210/pdb2bzd/pdb
• Related: 1EUR 1EUS 1EUT 1EUU 1W8N 1W8O 1WCQ 2BER 2BQ9
• Descriptor: BACTERIAL SIALIDASE, SODIUM ION, beta-D-galactopyranose, ... (5 entities in total)
• Functional Keywords: sialidase, hydrolase, carbohydrate binding module, glycosidase
• Biological source: MICROMONOSPORA VIRIDIFACIENS
• Cellular location: Secreted: Q02834
• Total number of polymer chains: 3
• Total formula weight: 193607.51

Authors

Newstead, S.L.,Taylor, G. (deposition date: 2005-08-16, release date: 2005-08-19, Last modification date: 2024-11-20)

Primary citation

Newstead, S.L.,Watson, J.N.,Bennet, A.J.,Taylor, G.
Galactose Recognition by the Carbohydrate-Binding Module of a Bacterial Sialidase.
Acta Crystallogr.,Sect.D, 61:1483-, 2005

PubMed Abstract: 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.

PubMed: 16239725
DOI: 10.1107/S0907444905026132

Experimental method

X-RAY DIFFRACTION (2 Å)