1pby: Difference between revisions
New page: left|200px<br /><applet load="1pby" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pby, resolution 1.70Å" /> '''Structure of the Phe... |
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[[Image:1pby.gif|left|200px]]<br /><applet load="1pby" size=" | [[Image:1pby.gif|left|200px]]<br /><applet load="1pby" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pby, resolution 1.70Å" /> | caption="1pby, resolution 1.70Å" /> | ||
'''Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution'''<br /> | '''Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution'''<br /> | ||
==Overview== | ==Overview== | ||
The 109 kDa quinohemoprotein amine dehydrogenase (QHNDH) from Paracoccus | 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. | ||
==About this Structure== | ==About this Structure== | ||
1PBY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with HEM and TBU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] Full crystallographic information is available from [http:// | 1PBY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=TBU:'>TBU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ikeda, T.]] | [[Category: Ikeda, T.]] | ||
[[Category: Kano, K.]] | [[Category: Kano, K.]] | ||
[[Category: Mathews, F | [[Category: Mathews, F S.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: TBU]] | [[Category: TBU]] | ||
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[[Category: quinohemoprotein]] | [[Category: quinohemoprotein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:18 2008'' | ||
Revision as of 15:27, 21 February 2008
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Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution
OverviewOverview
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.
About this StructureAbout this Structure
1PBY is a Protein complex structure of sequences from Paracoccus denitrificans with and as ligands. Active as Amine dehydrogenase, with EC number 1.4.99.3 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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