2v5j: Difference between revisions

Revision as of 14:23, 27 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:2v5j.png

Template:STRUCTURE 2v5j

APO CLASS II ALDOLASE HPCHAPO CLASS II ALDOLASE HPCH

Template:ABSTRACT PUBMED 17881002

About this StructureAbout this Structure

2V5J is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli., Rea D, Fulop V, Bugg TD, Roper DI, J Mol Biol. 2007 Nov 2;373(4):866-76. Epub 2007 Jun 26. PMID:17881002

Page seeded by OCA on Sun Jul 27 14:23:22 2008

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OCA

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-[[Image:2v5j.jpg|left|200px]]
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 {{STRUCTURE_2v5j|  PDB=2v5j  |  SCENE=  }}
-'''APO CLASS II ALDOLASE HPCH'''
+===APO CLASS II ALDOLASE HPCH===
-==Overview==
+<!--
-Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues.
+The line below this paragraph, {{ABSTRACT_PUBMED_17881002}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17881002 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17881002}}
 ==About this Structure==
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 [[Category: Homoprotocatechuate]]
 [[Category: Lyase]]
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