1otf

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[[Image:1otf.jpg|left|200px]]
 
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==4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM==
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The line below this paragraph, containing "STRUCTURE_1otf", creates the "Structure Box" on the page.
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<StructureSection load='1otf' size='340' side='right'caption='[[1otf]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1otf| PDB=1otf | SCENE= }}
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</table>
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== Function ==
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'''4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM'''
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[https://www.uniprot.org/uniprot/4OT_PSEUF 4OT_PSEUF] Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1otf_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1OTF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTF OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</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].
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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://www.ncbi.nlm.nih.gov/pubmed/8547259 8547259]
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<div style="clear:both"></div>
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[[Category: Pseudomonas sp.]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Dauter, Z.]]
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[[Category: Large Structures]]
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[[Category: Davies, G J.]]
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[[Category: Pseudomonas sp. CF600]]
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[[Category: Dodson, E J.]]
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[[Category: Dauter Z]]
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[[Category: Roper, D I.]]
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[[Category: Davies GJ]]
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[[Category: Subramanya, H S.]]
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[[Category: Dodson EJ]]
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[[Category: Wigley, D B.]]
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[[Category: Roper DI]]
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[[Category: Wilson, K S.]]
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[[Category: Subramanya HS]]
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[[Category: Tautomerase]]
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[[Category: Wigley DB]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:15:45 2008''
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[[Category: Wilson KS]]

Current revision

4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM

PDB ID 1otf

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