1gtt: Difference between revisions
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|PDB= 1gtt |SIZE=350|CAPTION= <scene name='initialview01'>1gtt</scene>, resolution 1.70Å | |PDB= 1gtt |SIZE=350|CAPTION= <scene name='initialview01'>1gtt</scene>, resolution 1.70Å | ||
|SITE= <scene name='pdbsite=CA1:Ca+Binding+Site+For+Chain+D'>CA1</scene> | |SITE= <scene name='pdbsite=CA1:Ca+Binding+Site+For+Chain+D'>CA1</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtt OCA], [http://www.ebi.ac.uk/pdbsum/1gtt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gtt RCSB]</span> | |||
}} | }} | ||
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[[Category: Roper, D I.]] | [[Category: Roper, D I.]] | ||
[[Category: Tame, J R.H.]] | [[Category: Tame, J R.H.]] | ||
[[Category: aromatic hydrocarbons catabolism,]] | |||
[[Category: aromatic hydrocarbons catabolism]] | [[Category: bifunctional enzyme,multifunctional enzyme decarboxylase]] | ||
[[Category: bifunctional enzyme]] | |||
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:08 2008'' | ||
Revision as of 20:51, 30 March 2008
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| , resolution 1.70Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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