1iux: Difference between revisions

Revision as of 14:02, 1 July 2008

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File:1iux.png

Template:STRUCTURE 1iux

P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 9.4P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 9.4

Template:ABSTRACT PUBMED 8555229

About this StructureAbout this Structure

1IUX is a Single protein structure of sequence from Pseudomonas aeruginosa pao1. Full crystallographic information is available from OCA.

ReferenceReference

pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis., Gatti DL, Entsch B, Ballou DP, Ludwig ML, Biochemistry. 1996 Jan 16;35(2):567-78. PMID:8555229

Page seeded by OCA on Tue Jul 1 14:02:40 2008

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OCA

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 {{STRUCTURE_1iux|  PDB=1iux  |  SCENE=  }}
-'''P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 9.4'''
+===P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 9.4===
-==Overview==
+<!--
-Deprotonation of p-hydroxybenzoate to the phenolate and reprotonation of the hydroxylated dienone intermediate to form the product are essential steps in the reaction catalyzed by p-hydroxybenzoate hydroxylase (PHBH). The mechanism by which protons are transferred in these reactions is not obvious, because the substrate bound in the active site is isolated from solvent. Structure analyses of wild-type and mutant PHBH, with bound p-hydroxybenzoate or p-aminobenzoate, reveal a chain of proton donors and acceptors (the hydroxyl groups of Tyr201 and Tyr385, and two water molecules) that can connect the substrate 4-OH to His72, a surface residue. This chain could provide a pathway for proton transfer to and from the substrate. Using various combinations of pH and substrates, we show that in crystalline PHBH ionizable groups in the chain may rotate and change hydrogen-bond orientation. Molecular dynamics simulations have been used to predict the preferred orientation of hydrogen bonds in the chain as a function of the ionization states of substrate and His72. The calculations suggest that changes in the ionization state of the substrate could be associated with changes in orientation of the hydrogen bonds in the chain. Transfer of water between the chain of proton donors and the solvent also appears to be an essential part of the mechanism that provides reversible transfer of protons during the hydroxylation reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_8555229}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8555229}}
 ==About this Structure==
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 [[Category: Aromatic hydrocarbons catabolism]]
 [[Category: Oxidoreducatase]]
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