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New page: left|200px<br /><applet load="1otg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1otg, resolution 2.1Å" /> '''5-CARBOXYMETHYL-2-HYD...
 
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[[Image:1otg.jpg|left|200px]]<br /><applet load="1otg" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1otg, resolution 2.1&Aring;" />
'''5-CARBOXYMETHYL-2-HYDROXYMUCONATE ISOMERASE'''<br />


==Overview==
==5-CARBOXYMETHYL-2-HYDROXYMUCONATE ISOMERASE==
5-Carboxymethyl-2-hydroxymuconate isomerase (CHMI) and 4-oxalocrotonate, tautomerase (4-OT) are enzymes that catalyze the isomerization of, unsaturated ketones. They share a common enzyme mechanism, although they, show a preference for different substrates. There is no apparent sequence, homology between the enzymes. To investigate the molecular mechanism and, the basis for their substrate specificity, we have determined the crystal, structures of the two enzymes at high resolution. 4-OT is hexameric, with, the subunits arranged with 32 symmetry. CHMI is trimeric and has extensive, contacts between subunits, which include secondary structural elements., The central core of the CHMI monomer has a fold similar to a 4-OT dimer, but the secondary structural elements that form the subunit contacts, around the 3-fold axis are different in the two enzymes. The region of, greatest similarity between the two enzymes is a large pocket that is, proposed to be the active site. The enzymes appear to operate via a, "one-base" mechanism, and the possible role of residues in this pocket is, discussed in view of this idea. Finally, the molecular basis for substrate, specificity in the two enzymes is discussed.
<StructureSection load='1otg' size='340' side='right'caption='[[1otg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1otg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_C Escherichia coli C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OTG FirstGlance]. <br>
1OTG 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OTG 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]] 2.1&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1otg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otg OCA], [https://pdbe.org/1otg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1otg RCSB], [https://www.ebi.ac.uk/pdbsum/1otg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1otg ProSAT]</span></td></tr>
Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases., Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB, Biochemistry. 1996 Jan 23;35(3):792-802. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8547259 8547259]
</table>
[[Category: Escherichia coli]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/HPCD_ECOLX HPCD_ECOLX] Transforms 5-carboxymethyl-2-hydroxy-muconic acid (CHM) into 5-oxo-pent-3-ene-1,2,5-tricarboxylic acid (OPET).
[[Category: Dauter, Z.]]
== Evolutionary Conservation ==
[[Category: Davies, G.J.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Dodson, E.J.]]
Check<jmol>
[[Category: Roper, D.I.]]
  <jmolCheckbox>
[[Category: Subramanya, H.S.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1otg_consurf.spt"</scriptWhenChecked>
[[Category: Wigley, D.B.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Wilson, K.S.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: SO4]]
  </jmolCheckbox>
[[Category: hydroxymuconate]]
</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=1otg ConSurf].
 
<div style="clear:both"></div>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:11:11 2007''
__TOC__
</StructureSection>
[[Category: Escherichia coli C]]
[[Category: Large Structures]]
[[Category: Dauter Z]]
[[Category: Davies GJ]]
[[Category: Dodson EJ]]
[[Category: Roper DI]]
[[Category: Subramanya HS]]
[[Category: Wigley DB]]
[[Category: Wilson KS]]

Latest revision as of 08:03, 14 February 2024

5-CARBOXYMETHYL-2-HYDROXYMUCONATE ISOMERASE

1otg, resolution 2.10Å

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