1b0m

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[[Image:1b0m.gif|left|200px]]
 
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{{Structure
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==ACONITASE R644Q:FLUOROCITRATE COMPLEX==
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|PDB= 1b0m |SIZE=350|CAPTION= <scene name='initialview01'>1b0m</scene>, resolution 2.50&Aring;
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<StructureSection load='1b0m' size='340' side='right'caption='[[1b0m]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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<table><tr><td colspan='2'>[[1b0m]] 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=1atq 1atq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B0M FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE=
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<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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0m OCA], [https://pdbe.org/1b0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b0m RCSB], [https://www.ebi.ac.uk/pdbsum/1b0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0m ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0m OCA], [http://www.ebi.ac.uk/pdbsum/1b0m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0m RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ACON_PIG ACON_PIG] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b0/1b0m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1b0m ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''ACONITASE R644Q:FLUOROCITRATE COMPLEX'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1b0m" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Aconitase 3D structures|Aconitase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1B0M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry 1ATQ. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0M OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Aconitate hydratase]]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Lauble, H.]]
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[[Category: Lauble H]]
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[[Category: Lloyd, S J.]]
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[[Category: Lloyd SJ]]
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[[Category: Prasad, G S.]]
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[[Category: Prasad GS]]
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[[Category: Stout, C D.]]
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[[Category: Stout CD]]
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[[Category: aconitase r644q]]
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[[Category: fluorocitrate complex]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:28 2008''
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Current revision

ACONITASE R644Q:FLUOROCITRATE COMPLEX

PDB ID 1b0m

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