1gtt: Difference between revisions
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==Overview== | ==Overview== | ||
The structure of the bifunctional enzyme HpcE (OPET decarboxylase/HHDD | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dodson, E | [[Category: Dodson, E J.]] | ||
[[Category: Namba, K.]] | [[Category: Namba, K.]] | ||
[[Category: Roper, D | [[Category: Roper, D I.]] | ||
[[Category: Tame, J | [[Category: Tame, J R.H.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: aromatic hydrocarbons catabolism]] | [[Category: aromatic hydrocarbons catabolism]] | ||
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[[Category: multifunctional enzyme decarboxylase]] | [[Category: multifunctional enzyme decarboxylase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:59 2008'' | ||
Revision as of 13:53, 21 February 2008
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CRYSTAL STRUCTURE OF HPCE
OverviewOverview
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.
About this StructureAbout this Structure
1GTT is a Single protein structure of sequence from Escherichia coli with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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