1gtt: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gtt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GTT FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gtt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GTT FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i7o|1i7o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i7o|1i7o]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1gtt RCSB], [http://www.ebi.ac.uk/pdbsum/1gtt PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1gtt RCSB], [http://www.ebi.ac.uk/pdbsum/1gtt PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Dodson, E J | [[Category: Dodson, E J]] | ||
[[Category: Namba, K | [[Category: Namba, K]] | ||
[[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]] | [[Category: Bifunctional enzyme]] | ||
Revision as of 22:10, 22 December 2014
CRYSTAL STRUCTURE OF HPCECRYSTAL STRUCTURE OF HPCE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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