2bwm

From Proteopedia

Revision as of 14:45, 30 October 2007

1.8A CRYSTAL STRUCTURE OF OF PSATHYRELLA VELUTINA LECTIN IN COMPLEX WITH METHYL 2-ACETAMIDO-1,2-DIDEOXY-1-SELENO-BETA-D-GLUCOPYRANOSIDE

Overview

The lectin from the mushroom Psathyrella velutina recognises specifically, N-acetylglucosamine and N-acetylneuraminic acid containing glycans. The, crystal structure of the 401 amino acid residue lectin shows that it, adopts a very regular seven-bladed beta-propeller fold with the N-terminal, region tucked into the central cavity around the pseudo 7-fold axis. In, the complex with N-acetylglucosamine, six monosaccharides are bound in, pockets located between two consecutive propeller blades. Due to the, repeats shown by the sequence the binding sites are very similar. Five, hydrogen bonds between the protein and the sugar hydroxyl and N-acetyl, groups stabilize the complex, together with the hydrophobic interactions, with a conserved tyrosine and histidine. The complex with, ... [(full description)]

About this Structure

2BWM is a [Single protein] structure of sequence from [Lacrymaria velutina] with CA, SO4, SNG and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium., Cioci G, Mitchell EP, Chazalet V, Debray H, Oscarson S, Lahmann M, Gautier C, Breton C, Perez S, Imberty A, J Mol Biol. 2006 Apr 14;357(5):1575-91. Epub 2006 Feb 6. PMID:16497330

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