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[[Image:1c96.gif|left|200px]]
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{{STRUCTURE_1c96|  PDB=1c96  |  SCENE=  }}
'''S642A:CITRATE COMPLEX OF ACONITASE'''


==S642A:CITRATE COMPLEX OF ACONITASE==
<StructureSection load='1c96' size='340' side='right'caption='[[1c96]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1c96]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The May 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Aconitase and Iron Regulatory Protein 1''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_5 10.2210/rcsb_pdb/mom_2007_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C96 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</td></tr>
<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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c96 OCA], [https://pdbe.org/1c96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c96 RCSB], [https://www.ebi.ac.uk/pdbsum/1c96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c96 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACON_BOVIN ACON_BOVIN] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c96_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1c96 ConSurf].
<div style="clear:both"></div>
<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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1C96 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The following page contains interesting information on the relation of 1C96 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb89_1.html Aconitase and Iron Regulatory Protein 1]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C96 OCA].
</div>
<div class="pdbe-citations 1c96" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/10631981 10631981]
*[[Aconitase 3D structures|Aconitase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aconitase and Iron Regulatory Protein 1]]
[[Category: Aconitase and Iron Regulatory Protein 1]]
[[Category: Aconitate hydratase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Lauble, H.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Lloyd, S J.]]
[[Category: Lauble H]]
[[Category: Prasad, G S.]]
[[Category: Lloyd SJ]]
[[Category: Stout, C D.]]
[[Category: Prasad GS]]
[[Category: 3d-structure]]
[[Category: Stout CD]]
[[Category: 4fe-4]]
[[Category: Iron-sulfur]]
[[Category: Lyase]]
[[Category: Mitochondrion]]
[[Category: Transit peptide]]
[[Category: Tricarboxylic acid cycle]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:29:00 2008''
Retrieved from "https://proteopedia.org/1c96"