2jbw

From Proteopedia

Revision as of 10:11, 30 October 2007

CRYSTAL STRUCTURE OF THE 2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE.

Overview

The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase from the, nicotine-degradation pathway of Arthrobacter nicotinovorans was, crystallized and the structure was determined by an X-ray diffraction, analysis at 2.1 A resolution. The enzyme belongs to the, alpha/beta-hydrolase family as derived from the chain-fold and from the, presence of a catalytic triad with its oxyanion hole at the common, position. This relationship assigns a pocket lined by the catalytic triad, as the active center. The asymmetric unit contains two C(2)-symmetric, dimer molecules, each adopting a specific conformation. One dimer forms a, more spacious active center pocket and the other a smaller one, suggesting, an induced-fit. All of the currently established C-C bond cleaving, alpha/beta-hydrolases are from ... [(full description)]

About this Structure

2JBW is a [Single protein] structure of sequence from [Arthrobacter nicotinovorans] with NA as [ligand]. Structure known Active Site: TRI. Full crystallographic information is available from [OCA].

Reference

Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation., Schleberger C, Sachelaru P, Brandsch R, Schulz GE, J Mol Biol. 2007 Mar 23;367(2):409-18. Epub 2006 Dec 30. PMID:17275835

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