2be9

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(New page: 200px<br /><applet load="2be9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2be9, resolution 2.60&Aring;" /> '''Crystal structure of...)
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[[Image:2be9.jpg|left|200px]]<br /><applet load="2be9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2be9, resolution 2.60&Aring;" />
 
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'''Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius'''<br />
 
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==Overview==
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==Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius==
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Aspartate carbamoyltransferase (ATCase) is a model enzyme for, understanding allosteric effects. The dodecameric complex exists in two, main states (T and R) that differ substantially in their quaternary, structure and their affinity for various ligands. Many hypotheses have, resulted from the structure of the Escherichia coli ATCase, but so far, other crystal structures to test these have been lacking. Here, we present, the tertiary and quaternary structure of the T state ATCase of the, hyperthermophilic archaeon Sulfolobus acidocaldarius (SaATC(T)), determined by X-ray crystallography to 2.6A resolution. The quaternary, structure differs from the E.coli ATCase, by having altered interfaces, between the catalytic (C) and regulatory (R) subunits, and the presence of, a novel C1-R2 type interface. Conformational differences in the 240 s loop, region of the C chain and the C-terminal region of the R chain affect, intersubunit and interdomain interfaces implicated previously in the, allosteric behavior of E.coli ATCase. The allosteric-zinc binding domain, interface is strengthened at the expense of a weakened R1-C4 type, interface. The increased hydrophobicity of the C1-R1 type interface may, stabilize the quaternary structure. Catalytic trimers of the, S.acidocaldarius ATCase are unstable due to a drastic weakening of the, C1-C2 interface. The hyperthermophilic ATCase presents an interesting, example of how an allosteric enzyme can adapt to higher temperatures. The, structural rearrangement of this thermophilic ATCase may well promote its, thermal stability at the expense of changes in the allosteric behavior.
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<StructureSection load='2be9' size='340' side='right'caption='[[2be9]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2be9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BE9 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]] 2.6&#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=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2be9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2be9 OCA], [https://pdbe.org/2be9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2be9 RCSB], [https://www.ebi.ac.uk/pdbsum/2be9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2be9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRB_SULAC PYRB_SULAC]
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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/be/2be9_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=2be9 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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Aspartate carbamoyltransferase (ATCase) is a paradigm for allosteric regulation of enzyme activity. B-class ATCases display very similar homotropic allosteric behaviour, but differ extensively in their heterotropic patterns. The ATCase from the thermoacidophilic archaeon Sulfolobus acidocaldarius, for example, is strongly activated by its metabolic pathway's end product CTP, in contrast with Escherichia coli ATCase which is inhibited by CTP. To investigate the structural basis of this property, we have solved the crystal structure of the S. acidocaldarius enzyme in complex with CTP. Structure comparison reveals that effector binding does not induce similar large-scale conformational changes as observed for the E. coli ATCase. However, shifts in sedimentation coefficients upon binding of the bi-substrate analogue PALA show the existence of structurally distinct allosteric states. This suggests that the so-called "Nucleotide-Perturbation model" for explaining heterotropic allosteric behaviour, which is based on global conformational strain, is not a general mechanism of B-class ATCases.
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==About this Structure==
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Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP.,De Vos D, Xu Y, Aerts T, Van Petegem F, Van Beeumen JJ Biochem Biophys Res Commun. 2008 Jul 18;372(1):40-4. Epub 2008 May 12. PMID:18477471<ref>PMID:18477471</ref>
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2BE9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius] with ZN, SO4 and CTP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BE9 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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Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius., De Vos D, Van Petegem F, Remaut H, Legrain C, Glansdorff N, Van Beeumen JJ, J Mol Biol. 2004 Jun 11;339(4):887-900. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15165857 15165857]
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</div>
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[[Category: Aspartate carbamoyltransferase]]
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<div class="pdbe-citations 2be9" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Sulfolobus acidocaldarius]]
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[[Category: Beeumen, J.Van.]]
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[[Category: Savvides, S.N.]]
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[[Category: Vos, D.De.]]
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[[Category: CTP]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: allosteric]]
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[[Category: atcase]]
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[[Category: ctp complex]]
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[[Category: holoenzyme]]
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[[Category: hyperthermophilic]]
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[[Category: temperature]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:45:33 2007''
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==See Also==
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*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 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: Sulfolobus acidocaldarius]]
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[[Category: De Vos D]]
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[[Category: Savvides SN]]
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[[Category: Van Beeumen JJ]]

Current revision

Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius

PDB ID 2be9

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