2ibp

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(New page: 200px<br /><applet load="2ibp" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ibp, resolution 1.60&Aring;" /> '''Crystal Structure of...)
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[[Image:2ibp.jpg|left|200px]]<br /><applet load="2ibp" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ibp, resolution 1.60&Aring;" />
 
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'''Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum'''<br />
 
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==Overview==
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==Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum==
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A growing number of organisms have been discovered inhabiting extreme, environments, including temperatures in excess of 100 degrees C. How, cellular proteins from such organisms retain their native folds under, extreme conditions is still not fully understood. Recent computational and, structural studies have identified disulfide bonding as an important, mechanism for stabilizing intracellular proteins in certain thermophilic, microbes. Here, we present the first proteomic analysis of intracellular, disulfide bonding in the hyperthermophilic archaeon Pyrobaculum, aerophilum. Our study reveals that the utilization of disulfide bonds, extends beyond individual proteins to include many protein-protein, complexes. We report the 1.6 A crystal structure of one such complex, a, citrate synthase homodimer. The structure contains two intramolecular, disulfide bonds, one per subunit, which result in the cyclization of each, protein chain in such a way that the two chains are topologically, interlinked, rendering them inseparable. This unusual feature emphasizes, the variety and sophistication of the molecular mechanisms that can be, achieved by evolution.
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<StructureSection load='2ibp' size='340' side='right'caption='[[2ibp]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ibp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IBP FirstGlance]. <br>
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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]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=2ibp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibp OCA], [https://pdbe.org/2ibp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ibp RCSB], [https://www.ebi.ac.uk/pdbsum/2ibp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ibp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8ZWP2_PYRAE Q8ZWP2_PYRAE]
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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/ib/2ibp_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=2ibp 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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A growing number of organisms have been discovered inhabiting extreme environments, including temperatures in excess of 100 degrees C. How cellular proteins from such organisms retain their native folds under extreme conditions is still not fully understood. Recent computational and structural studies have identified disulfide bonding as an important mechanism for stabilizing intracellular proteins in certain thermophilic microbes. Here, we present the first proteomic analysis of intracellular disulfide bonding in the hyperthermophilic archaeon Pyrobaculum aerophilum. Our study reveals that the utilization of disulfide bonds extends beyond individual proteins to include many protein-protein complexes. We report the 1.6 A crystal structure of one such complex, a citrate synthase homodimer. The structure contains two intramolecular disulfide bonds, one per subunit, which result in the cyclization of each protein chain in such a way that the two chains are topologically interlinked, rendering them inseparable. This unusual feature emphasizes the variety and sophistication of the molecular mechanisms that can be achieved by evolution.
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==About this Structure==
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Discovery of a thermophilic protein complex stabilized by topologically interlinked chains.,Boutz DR, Cascio D, Whitelegge J, Perry LJ, Yeates TO J Mol Biol. 2007 May 18;368(5):1332-44. Epub 2007 Mar 6. PMID:17395198<ref>PMID:17395198</ref>
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2IBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBP OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Discovery of a thermophilic protein complex stabilized by topologically interlinked chains., Boutz DR, Cascio D, Whitelegge J, Perry LJ, Yeates TO, J Mol Biol. 2007 May 18;368(5):1332-44. Epub 2007 Mar 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17395198 17395198]
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</div>
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[[Category: Citrate (Si)-synthase]]
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<div class="pdbe-citations 2ibp" style="background-color:#fffaf0;"></div>
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[[Category: Pyrobaculum aerophilum]]
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[[Category: Single protein]]
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[[Category: Boutz, D.R.]]
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[[Category: Cascio, D.]]
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[[Category: Yeates, T.O.]]
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[[Category: ACT]]
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[[Category: MG]]
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[[Category: catenane]]
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[[Category: citrate synthase]]
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[[Category: disulfide bond]]
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[[Category: homodimer]]
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[[Category: thermophilic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:16:24 2008''
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==See Also==
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*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pyrobaculum aerophilum str. IM2]]
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[[Category: Boutz DR]]
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[[Category: Cascio D]]
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[[Category: Yeates TO]]

Current revision

Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum

PDB ID 2ibp

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