1gtt: Difference between revisions
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'''CRYSTAL STRUCTURE OF HPCE''' | '''CRYSTAL STRUCTURE OF HPCE''' | ||
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[[Category: Roper, D I.]] | [[Category: Roper, D I.]] | ||
[[Category: Tame, J R.H.]] | [[Category: Tame, J R.H.]] | ||
[[Category: | [[Category: Aromatic hydrocarbons catabolism]] | ||
[[Category: | [[Category: Bifunctional enzyme,multifunctional enzyme decarboxylase]] | ||
[[Category: | [[Category: Isomerase]] | ||
[[Category: | [[Category: Lyase]] | ||
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Revision as of 18:00, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 18:00:00 2008