1c97

<StructureSection load='1c97' size='340' side='right' caption='[[1c97]], [[Resolution|resolution]] 1.98&Aring;' scene=''>

<table><tr><td colspan='2'>[[1c97]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C97 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ICT:ISOCITRIC+ACID'>ICT</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c96|1c96]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c97 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c97 RCSB], [http://www.ebi.ac.uk/pdbsum/1c97 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ACON_BOVIN ACON_BOVIN]] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c97_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Aconitase|Aconitase]]

[[Category: Aconitate hydratase]]

[[Category: Lauble, H]]

[[Category: Lloyd, S J]]

[[Category: Prasad, G S]]

[[Category: Stout, C D]]

[[Category: Iron-sulfur]]

[[Category: Tricarboxylic acid cycle]]