2jbs
From Proteopedia
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Revision as of 15:24, 30 October 2007
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STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNII
Overview
p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii is a, two-component system consisting of a NADH-dependent FMN reductase and a, monooxygenase (C2) that uses reduced FMN as substrate. The crystal, structures of C2 in the ligand-free and substrate-bound forms reveal a, preorganized pocket that binds reduced FMN without large conformational, changes. The Phe-266 side chain swings out to provide the space for, binding p-hydroxyphenylacetate that is oriented orthogonal to the flavin, ring. The geometry of the substrate-binding site of C2 is significantly, different from that of p-hydroxybenzoate hydroxylase, a single-component, flavoenzyme that catalyzes a similar reaction. The C2 overall structure, resembles the folding of medium-chain acyl-CoA dehydrogenase. An, outstanding ... [(full description)]
About this Structure
2JBS is a [Single protein] structure of sequence from [Acinetobacter baumannii] with FMN as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of the monooxygenase component of a two-component flavoprotein monooxygenase., Alfieri A, Fersini F, Ruangchan N, Prongjit M, Chaiyen P, Mattevi A, Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1177-82. Epub 2007 Jan 16. PMID:17227849
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