1c97: Difference between revisions

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[[Image:1c97.gif|left|200px]]
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{{STRUCTURE_1c97|  PDB=1c97  |  SCENE=  }}
'''S642A:ISOCITRATE COMPLEX OF ACONITASE'''


==S642A:ISOCITRATE COMPLEX OF ACONITASE==
<StructureSection load='1c97' size='340' side='right'caption='[[1c97]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1c97]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1C97 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]] 1.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ICT:ISOCITRIC+ACID'>ICT</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=1c97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c97 OCA], [https://pdbe.org/1c97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c97 RCSB], [https://www.ebi.ac.uk/pdbsum/1c97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c97 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/c9/1c97_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=1c97 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>
1C97 is a [[Single protein]] structure of 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].
</div>
<div class="pdbe-citations 1c97" 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]]
[[Category: Aconitate hydratase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Lauble, H.]]
[[Category: Lauble H]]
[[Category: Lloyd, S J.]]
[[Category: Lloyd SJ]]
[[Category: Prasad, G S.]]
[[Category: Prasad GS]]
[[Category: Stout, C D.]]
[[Category: Stout CD]]
[[Category: 3d-structure]]
[[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 12:29:01 2008''

Latest revision as of 05:32, 13 August 2026

S642A:ISOCITRATE COMPLEX OF ACONITASE

1c97, resolution 1.98Å

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