1b0k: Difference between revisions
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<StructureSection load='1b0k' size='340' side='right'caption='[[1b0k]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1b0k' size='340' side='right'caption='[[1b0k]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b0k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</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>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ACON_PIG ACON_PIG] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sus scrofa]] | ||
[[Category: Lauble | [[Category: Lauble H]] | ||
[[Category: Lloyd | [[Category: Lloyd SJ]] | ||
[[Category: Prasad | [[Category: Prasad GS]] | ||
[[Category: Stout | [[Category: Stout CD]] | ||
Latest revision as of 08:34, 9 August 2023
S642A:FLUOROCITRATE COMPLEX OF ACONITASES642A:FLUOROCITRATE COMPLEX OF ACONITASE
Structural highlights
FunctionACON_PIG 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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