1c96: Difference between revisions
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<StructureSection load='1c96' size='340' side='right' caption='[[1c96]], [[Resolution|resolution]] 1.81Å' scene=''> | <StructureSection load='1c96' size='340' side='right' caption='[[1c96]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c96]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1c96]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. The May 2007 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C96 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c97|1c97]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c97|1c97]]</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='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=1c96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c96 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c96 RCSB], [http://www.ebi.ac.uk/pdbsum/1c96 PDBsum]</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=1c96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c96 OCA], [http://pdbe.org/1c96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c96 RCSB], [http://www.ebi.ac.uk/pdbsum/1c96 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1c96" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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[[Category: Aconitase and Iron Regulatory Protein 1]] | [[Category: Aconitase and Iron Regulatory Protein 1]] | ||
[[Category: Aconitate hydratase]] | [[Category: Aconitate hydratase]] | ||
[[Category: | [[Category: Bovin]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Lauble, H]] | [[Category: Lauble, H]] | ||
Revision as of 21:36, 10 September 2015
S642A:CITRATE COMPLEX OF ACONITASES642A:CITRATE COMPLEX OF ACONITASE
Structural highlights
Function[ACON_BOVIN] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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 --> 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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