2bvg

From Proteopedia

Revision as of 14:44, 30 October 2007

CRYSTAL STRUCTURE OF 6-HYDOXY-D-NICOTINE OXIDASE FROM ARTHROBACTER NICOTINOVORANS. CRYSTAL FORM 1 (P21)

Overview

The crystal structure of 6-hydroxy-d-nicotine oxidase (EC 1.5.3.6) was, solved by X-ray diffraction analysis in three crystal forms at resolutions, up to 1.9 A. The enzyme is monomeric in solution and also in the mother, liquor but formed disulfide-dimers in all crystals. It belongs to the, p-cresol methylhydroxylase-vanillyl-alcohol oxidase family and contains an, FAD covalently bound to the polypeptide. The covalent bond of this enzyme, was the first for which a purely autocatalytic formation had been shown., In contrast to previous reports, the bond does not involve N(epsilon2), (N3) of His72 but the N(delta1) (N1) atom. The geometry of this reaction, is proposed and the autoflavinylation is discussed in the light of, homologous structures. The enzyme is specific for ... [(full description)]

About this Structure

2BVG is a [Single protein] structure of sequence from [Arthrobacter nicotinovorans] with FAD as [ligand]. Active as [(R)-6-hydroxynicotine oxidase], with EC number [1.5.3.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans., Koetter JW, Schulz GE, J Mol Biol. 2005 Sep 16;352(2):418-28. PMID:16095622

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