1t3q

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{{STRUCTURE_1t3q| PDB=1t3q | SCENE= }}
{{STRUCTURE_1t3q| PDB=1t3q | SCENE= }}
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'''Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86'''
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===Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86===
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==Overview==
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The soil bacterium Pseudomonas putida 86 uses quinoline as a sole source of carbon and energy. Quinoline 2-oxidoreductase (Qor) catalyzes the first metabolic step converting quinoline to 2-oxo-1,2-dihydroquinoline. Qor is a member of the molybdenum hydroxylases. The molybdenum ion is coordinated by two ene-dithiolate sulfur atoms, two oxo-ligands, and a catalytically crucial sulfido-ligand, whose position in the active site was controversial. The 1.8 A resolution crystal structure of Qor indicates that the sulfido-ligand occupies the equatorial position at the molybdenum ion. The structural comparison of Qor with the allopurinol-inhibited xanthine dehydrogenase from Rhodobacter capsulatus allows direct insight into the mechanism of substrate recognition and the identification of putative catalytic residues. The active site protein variants QorE743V and QorE743D were analyzed to assess the catalytic role of E743.
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(as it appears on PubMed at http://www.pubmed.gov), where 15296736 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15296736}}
==About this Structure==
==About this Structure==
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[[Category: Molybdenum]]
[[Category: Molybdenum]]
[[Category: Qor]]
[[Category: Qor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:55:23 2008''

Revision as of 18:55, 28 July 2008

Template:STRUCTURE 1t3q

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

Template:ABSTRACT PUBMED 15296736

About this Structure

1T3Q is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase., Bonin I, Martins BM, Purvanov V, Fetzner S, Huber R, Dobbek H, Structure. 2004 Aug;12(8):1425-35. PMID:15296736

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