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2jbw

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[[Image:2jbw.jpg|left|200px]]
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{{STRUCTURE_2jbw| PDB=2jbw | SCENE= }}
{{STRUCTURE_2jbw| PDB=2jbw | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE 2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE.'''
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===CRYSTAL STRUCTURE OF THE 2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE.===
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==Overview==
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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 bacterial meta-cleavage pathways for the degradation of aromatic compounds and cover their active center with a 40 residue lid placed between two adjacent strands of the beta-sheet. In contrast, the reported enzyme shields its active center with a 110 residue N-terminal domain, which is absent in the meta-cleavage hydrolases. Since neither the substrate nor an analogue could be bound in the crystals, the substrate was modeled into the active center using the oxyanion hole as a geometric constraint. The model was supported by enzymatic activity data of 11 point mutants and by the two dimer conformations suggesting an induced-fit. Moreover, the model assigned a major role for the large N-terminal domain that is specific to the reported enzyme. The proposal is consistent with the known data for the meta-cleavage hydrolases although it differs in that the reaction does not release alkenes but a hetero-aromatic compound in a retro-Friedel-Crafts acylation. Because the hydrolytic water molecule can be assigned to a geometrically suitable site that can be occupied in the presence of the substrate, the catalytic triad may not form a covalent acyl-enzyme intermediate but merely support a direct hydrolysis.
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(as it appears on PubMed at http://www.pubmed.gov), where 17275835 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17275835}}
==About this Structure==
==About this Structure==
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[[Category: Plasmid]]
[[Category: Plasmid]]
[[Category: Retro- friedel-crafts acylation]]
[[Category: Retro- friedel-crafts acylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:39:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:29:40 2008''

Revision as of 07:29, 28 July 2008

Image:2jbw.png

Template:STRUCTURE 2jbw

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

Template:ABSTRACT PUBMED 17275835

About this Structure

2JBW is a Single protein structure of sequence from Arthrobacter nicotinovorans. 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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