1oqf

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[[Image:1oqf.gif|left|200px]]
 
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==Crystal structure of the 2-methylisocitrate lyase==
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The line below this paragraph, containing "STRUCTURE_1oqf", creates the "Structure Box" on the page.
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<StructureSection load='1oqf' size='340' side='right'caption='[[1oqf]], [[Resolution|resolution]] 1.93&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'>[[1oqf]] is a 2 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=1OQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQF 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]] 1.93&#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=1oqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqf OCA], [https://pdbe.org/1oqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oqf RCSB], [https://www.ebi.ac.uk/pdbsum/1oqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqf ProSAT]</span></td></tr>
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{{STRUCTURE_1oqf| PDB=1oqf | SCENE= }}
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</table>
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== Function ==
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'''Crystal structure of the 2-methylisocitrate lyase'''
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[https://www.uniprot.org/uniprot/PRPB_ECOLI PRPB_ECOLI] Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate.<ref>PMID:11422389</ref> <ref>PMID:15723538</ref>
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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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Two crystal structures of the C123S mutant of 2-methylisocitrate lyase have been determined, one with the bound reaction products, Mg(2+)-pyruvate and succinate, and the second with a bound Mg(2+)-(2R,3S)-isocitrate inhibitor. Comparison with the structure of the wild-type enzyme in the unbound state reveals that the enzyme undergoes a conformational transition that sequesters the ligand from solvent, as previously observed for two other enzyme superfamily members, isocitrate lyase and phosphoenolpyruvate mutase. The binding modes reveal the determinants of substrate specificity and stereoselectivity, and the stringent specificity is verified in solution using various potential substrates. A model of bound 2-methylisocitrate has been developed based on the experimentally determined structures. We propose a catalytic mechanism involving an alpha-carboxy-carbanion intermediate/transition state, which is consistent with previous stereochemical experiments showing inversion of configuration at the C(3) of 2-methylisocitrate. Structure-based sequence analysis and phylogenic tree construction reveal determinants of substrate specificity, highlight nodes of divergence of families, and predict enzyme families with new functions.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/1oqf_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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1OQF is a [[Single protein]] structure of 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=1OQF 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=1oqf ConSurf].
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Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution., Liu S, Lu Z, Han Y, Melamud E, Dunaway-Mariano D, Herzberg O, Biochemistry. 2005 Mar 1;44(8):2949-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15723538 15723538]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Methylisocitrate lyase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Dunaway-Mariano D]]
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[[Category: Dunaway-Mariano, D.]]
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[[Category: Herzberg O]]
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[[Category: Herzberg, O.]]
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[[Category: Liu S]]
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[[Category: Liu, S.]]
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[[Category: Lu Z]]
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[[Category: Lu, Z.]]
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[[Category: S2F, Structure 2.Function Project.]]
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[[Category: Alpha-beta barrel]]
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[[Category: S2f]]
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[[Category: Structural genomic]]
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[[Category: Structure 2 function project]]
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[[Category: Swapped helix across a dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:09:32 2008''
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Current revision

Crystal structure of the 2-methylisocitrate lyase

PDB ID 1oqf

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