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2eb5

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{{STRUCTURE_2eb5| PDB=2eb5 | SCENE= }}
{{STRUCTURE_2eb5| PDB=2eb5 | SCENE= }}
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'''Crystal structure of HpcG complexed with oxalate'''
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===Crystal structure of HpcG complexed with oxalate===
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==Overview==
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HpcG catalyses the hydration of a carbon-carbon double bond without the aid of any cofactor other than a simple divalent metal ion such as Mg(2+). Since the substrate has a nearby carbonyl group, it is believed that it first isomerises to form a pair of conjugated double bonds in the enol tautomer before Michael addition of water. Previous chemical studies of the reaction, and that of the related enzyme MhpD, have failed to provide a clear picture of the mechanism. The substrate itself is unstable, preventing co-crystallisation or soaking of crystals, but oxalate is a strong competitive inhibitor. We have solved the crystal structure of the protein in the apo form, and with magnesium and oxalate bound. Modelling substrate into the active site suggests the attacking water molecule is not part of the metal coordination shell, in contrast to a previous proposal. Our model suggests that geometrically strained cis isomer intermediates do not lie on the reaction pathway, and that separate groups are involved in the isomerisation and hydration steps.
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(as it appears on PubMed at http://www.pubmed.gov), where 17559873 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17559873}}
==About this Structure==
==About this Structure==
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[[Category: Hydratase]]
[[Category: Hydratase]]
[[Category: Lyase]]
[[Category: Lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:15:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:30:44 2008''

Revision as of 00:30, 28 July 2008

Image:2eb5.png

Template:STRUCTURE 2eb5

Crystal structure of HpcG complexed with oxalate

Template:ABSTRACT PUBMED 17559873

About this Structure

2EB5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli., Izumi A, Rea D, Adachi T, Unzai S, Park SY, Roper DI, Tame JR, J Mol Biol. 2007 Jul 27;370(5):899-911. Epub 2007 May 10. PMID:17559873

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