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New page: left|200px<br /><applet load="1otf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1otf, resolution 1.9Å" /> '''4-OXALOCROTONATE TAUT...
 
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[[Image:1otf.jpg|left|200px]]<br /><applet load="1otf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1otf, resolution 1.9&Aring;" />
'''4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM'''<br />


==Overview==
==4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM==
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='1otf' size='340' side='right'caption='[[1otf]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1otf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._CF600 Pseudomonas sp. CF600]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OTF FirstGlance]. <br>
1OTF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OTF 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]] 1.9&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1otf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otf OCA], [https://pdbe.org/1otf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1otf RCSB], [https://www.ebi.ac.uk/pdbsum/1otf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1otf ProSAT]</span></td></tr>
==Reference==
</table>
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]
== Function ==
[[Category: Pseudomonas sp.]]
[https://www.uniprot.org/uniprot/4OT_PSEUF 4OT_PSEUF] Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Dauter, Z.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Davies, G.J.]]
Check<jmol>
[[Category: Dodson, E.J.]]
  <jmolCheckbox>
[[Category: Roper, D.I.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1otf_consurf.spt"</scriptWhenChecked>
[[Category: Subramanya, H.S.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Wigley, D.B.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Wilson, K.S.]]
  </jmolCheckbox>
[[Category: tautomerase]]
</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=1otf ConSurf].
 
<div style="clear:both"></div>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:11:06 2007''
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas sp. CF600]]
[[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 08:02, 14 February 2024

4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM

1otf, resolution 1.90Å

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