2xed

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{{STRUCTURE_2xed| PDB=2xed | SCENE= }}
 
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===NOCARDIA FARCINICA MALEATE CIS-TRANS ISOMERASE C194S MUTANT WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE===
 
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{{ABSTRACT_PUBMED_20677745}}
 
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==About this Structure==
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==Nocardia farcinica maleate cis-trans isomerase C194S mutant with a covalently bound succinylcysteine intermediate==
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[[2xed]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Nocardia_farcinica Nocardia farcinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XED OCA].
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<StructureSection load='2xed' size='340' side='right'caption='[[2xed]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xed]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Nocardia_farcinica_IFM_10152 Nocardia farcinica IFM 10152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XED FirstGlance]. <br>
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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]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></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=2xed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xed OCA], [https://pdbe.org/2xed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xed RCSB], [https://www.ebi.ac.uk/pdbsum/2xed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xed ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAIA_NOCFA MAIA_NOCFA] Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Shows a strict specificity for maleate, with no activity detected toward structurally related substrates including citraconate, mesaconate, dimethylmaleate, and maleamide.<ref>PMID:20677745</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xe/2xed_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2xed ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.
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==Reference==
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A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase.,Fisch F, Fleites CM, Delenne M, Baudendistel N, Hauer B, Turkenburg JP, Hart S, Bruce NC, Grogan G J Am Chem Soc. 2010 Aug 2. PMID:20677745<ref>PMID:20677745</ref>
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<ref group="xtra">PMID:020677745</ref><references group="xtra"/><references/>
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[[Category: Maleate isomerase]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Nocardia farcinica]]
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</div>
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[[Category: Baudendistel, N.]]
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<div class="pdbe-citations 2xed" style="background-color:#fffaf0;"></div>
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[[Category: Bruce, N C.]]
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== References ==
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[[Category: Fisch, F.]]
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<references/>
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[[Category: Grogan, G.]]
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__TOC__
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[[Category: Hart, S.]]
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</StructureSection>
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[[Category: Hauer, B.]]
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[[Category: Large Structures]]
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[[Category: Martinez-Fleites, C.]]
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[[Category: Nocardia farcinica IFM 10152]]
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[[Category: Turkenburg, J P.]]
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[[Category: Baudendistel N]]
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[[Category: Cofactor-independent cis-trans isomerase]]
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[[Category: Bruce NC]]
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[[Category: Isomerase]]
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[[Category: Fisch F]]
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[[Category: Nicotinic acid catabolism]]
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[[Category: Grogan G]]
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[[Category: Hart S]]
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[[Category: Hauer B]]
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[[Category: Martinez-Fleites C]]
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[[Category: Turkenburg JP]]

Current revision

Nocardia farcinica maleate cis-trans isomerase C194S mutant with a covalently bound succinylcysteine intermediate

PDB ID 2xed

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