1kwc: Difference between revisions

Revision as of 11:08, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kwc.png

Template:STRUCTURE 1kwc

The His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenylThe His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenyl

Template:ABSTRACT PUBMED 12206778

About this StructureAbout this Structure

1KWC is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase., Sato N, Uragami Y, Nishizaki T, Takahashi Y, Sazaki G, Sugimoto K, Nonaka T, Masai E, Fukuda M, Senda T, J Mol Biol. 2002 Aug 23;321(4):621-36. PMID:12206778

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1kwc.jpg|left|200px]]
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 {{STRUCTURE_1kwc|  PDB=1kwc  |  SCENE=  }}
-'''The His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenyl'''
+===The His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenyl===
-==Overview==
+<!--
-BphC derived from Pseudomonas sp. strain KKS102 is an extradiol-cleaving catecholic dioxygenase. This enzyme contains a non-heme iron atom and plays an important role in degrading biphenyl/polychlorinated biphenyls (PCBs) in the microbe. To elucidate detailed structures of BphC reaction intermediates, crystal structures of the substrate-free form, the BphC-substrate complex, and the BphC-substrate-NO (nitric oxide) complex were determined. These crystal structures revealed (1) the binding site of the O(2) molecule in the coordination sphere and (2) conformational changes of His194 during the catalytic reaction. On the basis of these findings, we propose a catalytic mechanism for the extradiol-cleaving catecholic dioxygenase in which His194 seems to play three distinct roles. At the early stage of the catalytic reaction, His194 appears to act as a catalytic base, which likely deprotonates the hydroxyl group of the substrate. At the next stage, the protonated His194 seems to stabilize a negative charge on the O2 molecule located in the hydrophobic O2-binding cavity. Finally, protonated His194 seems to function as a proton donor, whose existence has been proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_12206778}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12206778 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12206778}}
 ==About this Structure==
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 [[Category: Uragami, Y.]]
 [[Category: Four time repetitions of the beta-alpha-beta-beta-beta motif]]
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