3b6d
From Proteopedia
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Crystal Structure of Streptomyces Cholesterol Oxidase H447Q/E361Q mutant (1.2A)
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
3B6D 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
Page seeded by OCA on Wed Jan 23 11:36:56 2008
