1pby: Difference between revisions

Revision as of 15:02, 28 July 2008

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File:1pby.png

Template:STRUCTURE 1pby

Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A ResolutionStructure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution

Template:ABSTRACT PUBMED 12925784

About this StructureAbout this Structure

1PBY is a Protein complex structure of sequences from Paracoccus denitrificans. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the phenylhydrazine adduct of the quinohemoprotein amine dehydrogenase from Paracoccus denitrificans at 1.7 A resolution., Datta S, Ikeda T, Kano K, Mathews FS, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1551-6. Epub 2003, Aug 19. PMID:12925784

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OCA

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-[[Image:1pby.gif|left|200px]]
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 {{STRUCTURE_1pby|  PDB=1pby  |  SCENE=  }}
-'''Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution'''
+===Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution===
-==Overview==
+<!--
-The 109 kDa quinohemoprotein amine dehydrogenase (QHNDH) from Paracoccus denitrificans contains a novel redox cofactor, cysteine tryptophylquinone (CTQ). This cofactor is derived from a pair of gene-encoded amino acids by post-translational modification and was previously identified and characterized within an 82-residue subunit by chemical methods and crystallographic analysis at 2.05 A resolution. It contains an orthoquinone moiety bound to the indole ring and catalyzes the oxidation of aliphatic and aromatic amines through formation of a Schiff-base intermediate involving one of the quinone O atoms. This paper reports the structural analysis of the complex of QHNDH with the enzyme inhibitor phenylhydrazine determined at 1.70 A resolution. The phenylhydrazone product is attached to the C6 position, identifying the O6 atom of CTQ as the site of Schiff-base formation as postulated by analogy to another amine-oxidizing enzyme, methylamine dehydrogenase. Furthermore, the inner N atom closest to the phenyl ring of phenylhydrazine forms a hydrogen bond to gammaAsp33 in the complex, lending support to the hypothesis that this residue serves as the active-site base for proton abstraction during catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12925784}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12925784 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12925784}}
 ==About this Structure==
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 [[Category: Amine dehydrogenase]]
 [[Category: Quinohemoprotein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:55:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:02:42 2008''