3b3r

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Revision as of 09:36, 23 January 2008

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spinqualitylabelsall models 3b3r, resolution 0.980Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Streptomyces cholesterol oxidase H447Q/E361Q mutant bound to glycerol (0.98A)

Overview

Two high-resolution structures of a double mutant of bacterial cholesterol, oxidase in the presence or absence of a ligand, glycerol, are presented, showing the trajectory of glycerol as it binds in a Michaelis complex-like, position in the active site. A group of three aromatic residues forces the, oxidized isoalloxazine moiety to bend along the N5-N10 axis as a response, to the binding of glycerol in the active site. Movement of these aromatic, residues is only observed in the glycerol-bound structure, indicating that, some tuning of the FAD redox potential is caused by the formation of the, Michaelis complex during regular catalysis. This structural study suggests, a possible mechanism of substrate-assisted flavin activation, improves our, understanding of the interplay between the enzyme, its flavin cofactor and, its substrate, and is of use to the future design of effective cholesterol, oxidase inhibitors.

About this Structure

3B3R is a Single protein structure of sequence from Streptomyces sp. with , and as ligands. Active as Cholesterol oxidase, with EC number 1.1.3.6 Full crystallographic information is available from OCA.

Reference

Distortion of flavin geometry is linked to ligand binding in cholesterol oxidase., Lyubimov AY, Heard K, Tang H, Sampson NS, Vrielink A, Protein Sci. 2007 Dec;16(12):2647-56. PMID:18029419

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