1b0k

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(New page: 200px<br /><applet load="1b0k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0k, resolution 2.50&Aring;" /> '''S642A:FLUOROCITRATE ...)
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[[Image:1b0k.jpg|left|200px]]<br /><applet load="1b0k" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1b0k, resolution 2.50&Aring;" />
 
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'''S642A:FLUOROCITRATE COMPLEX OF ACONITASE'''<br />
 
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==Overview==
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==S642A:FLUOROCITRATE COMPLEX OF ACONITASE==
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The crystal structure of the S642A mutant of mitochondrial aconitase (mAc), with citrate bound has been determined at 1.8 A resolution and 100 K to, capture this binding mode of substrates to the native enzyme. The 2.0 A, resolution, 100 K crystal structure of the S642A mutant with isocitrate, binding provides a control, showing that the Ser --&gt; Ala replacement does, not alter the binding of substrates in the active site. The aconitase, mechanism requires that the intermediate product, cis-aconitate, flip over, by 180 degrees about the C alpha-C beta double bond. Only one of these two, alternative modes of binding, that of the isocitrate mode, has been, previously visualized. Now, however, the structure revealing the citrate, mode of binding provides direct support for the proposed enzyme mechanism.
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<StructureSection load='1b0k' size='340' side='right'caption='[[1b0k]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b0k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1as9 1as9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B0K 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]] 2.5&#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=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=1b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0k OCA], [https://pdbe.org/1b0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b0k RCSB], [https://www.ebi.ac.uk/pdbsum/1b0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACON_PIG ACON_PIG] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
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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/b0/1b0k_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=1b0k 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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The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --&gt; Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism.
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==About this Structure==
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The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex.,Lloyd SJ, Lauble H, Prasad GS, Stout CD Protein Sci. 1999 Dec;8(12):2655-62. PMID:10631981<ref>PMID:10631981</ref>
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1B0K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with FLC, SF4 and O as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1AS9. Active as [http://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B0K OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex., Lloyd SJ, Lauble H, Prasad GS, Stout CD, Protein Sci. 1999 Dec;8(12):2655-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10631981 10631981]
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</div>
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[[Category: Aconitate hydratase]]
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<div class="pdbe-citations 1b0k" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
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[[Category: Lauble, H.]]
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[[Category: Lloyd, S.J.]]
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[[Category: Prasad, G.S.]]
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[[Category: Stout, C.D.]]
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[[Category: FLC]]
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[[Category: O]]
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[[Category: SF4]]
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[[Category: iron-sulfur]]
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[[Category: lyase]]
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[[Category: mitochondrion]]
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[[Category: transit peptide]]
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[[Category: tricarboxylic acid cycle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:15:33 2007''
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==See Also==
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*[[Aconitase 3D structures|Aconitase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sus scrofa]]
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[[Category: Lauble H]]
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[[Category: Lloyd SJ]]
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[[Category: Prasad GS]]
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[[Category: Stout CD]]

Current revision

S642A:FLUOROCITRATE COMPLEX OF ACONITASE

PDB ID 1b0k

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