1gtt

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{{STRUCTURE_1gtt| PDB=1gtt | SCENE= }}
{{STRUCTURE_1gtt| PDB=1gtt | SCENE= }}
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'''CRYSTAL STRUCTURE OF HPCE'''
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===CRYSTAL STRUCTURE OF HPCE===
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==Overview==
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The structure of the bifunctional enzyme HpcE (OPET decarboxylase/HHDD isomerase) from Escherichia coli shows that the protein consists of highly similar N and C terminal halves. Sequence matches suggest that this fold is widespread among different species, including man. Many of these homologues are uncharacterized but apparently connected with the metabolism of aromatic compounds. The domain shows similar topology to the C terminal domain of fumarylacetoacetate hydrolase (FAH), a functionally related enzyme, despite lacking significant overall sequence similarity. HpcE is known to catalyze two rather different reactions, and comparisons with FAH allow some tentative conclusions to be drawn about the active sites. Key mutations within the active site apparently allow enzymes with this fold to carry out a variety chemical processes.
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(as it appears on PubMed at http://www.pubmed.gov), where 11863436 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11863436}}
==About this Structure==
==About this Structure==
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[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Lyase]]
[[Category: Lyase]]
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Revision as of 03:04, 1 July 2008

Image:1gtt.png

Template:STRUCTURE 1gtt

CRYSTAL STRUCTURE OF HPCE

Template:ABSTRACT PUBMED 11863436

About this Structure

1GTT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold., Tame JR, Namba K, Dodson EJ, Roper DI, Biochemistry. 2002 Mar 5;41(9):2982-9. PMID:11863436

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