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[[Image:1gtt.gif|left|200px]]<br /><applet load="1gtt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gtt, resolution 1.70&Aring;" />
'''CRYSTAL STRUCTURE OF HPCE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF HPCE==
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.
<StructureSection load='1gtt' size='340' side='right'caption='[[1gtt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1gtt]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1GTT FirstGlance]. <br>
1GTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=CA1:Ca Binding Site For Chain D'>CA1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTT OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtt OCA], [https://pdbe.org/1gtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gtt RCSB], [https://www.ebi.ac.uk/pdbsum/1gtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gtt ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11863436 11863436]
</table>
== Function ==
[https://www.uniprot.org/uniprot/HPCE_ECOLX HPCE_ECOLX] Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it to OHED (2-oxo-hept-3-ene-1,7-dioate).<ref>PMID:8223600</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/1gtt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gtt ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dodson, E.J.]]
[[Category: Dodson EJ]]
[[Category: Namba, K.]]
[[Category: Namba K]]
[[Category: Roper, D.I.]]
[[Category: Roper DI]]
[[Category: Tame, J.R.H.]]
[[Category: Tame JRH]]
[[Category: CA]]
[[Category: aromatic hydrocarbons catabolism]]
[[Category: bifunctional enzyme]]
[[Category: isomerase]]
[[Category: lyase]]
[[Category: multifunctional enzyme decarboxylase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:35:54 2007''

Latest revision as of 14:24, 27 March 2024

CRYSTAL STRUCTURE OF HPCECRYSTAL STRUCTURE OF HPCE

Structural highlights

1gtt is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HPCE_ECOLX Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it to OHED (2-oxo-hept-3-ene-1,7-dioate).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Roper DI, Cooper RA. Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C. Eur J Biochem. 1993 Oct 15;217(2):575-80. PMID:8223600

1gtt, resolution 1.70Å

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