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| | <StructureSection load='2be9' size='340' side='right'caption='[[2be9]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2be9' size='340' side='right'caption='[[2be9]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2be9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. 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> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pg5|1pg5]]</div></td></tr>
| + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyrB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909]), pyrI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </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=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> | | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PYRI_SULAC PYRI_SULAC]] Involved in allosteric regulation of aspartate carbamoyltransferase (By similarity).
| + | [https://www.uniprot.org/uniprot/PYRB_SULAC PYRB_SULAC] |
| | == 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: Aspartate carbamoyltransferase]] | |
| - | [[Category: Atcc 33909]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beeumen, J J.Van]] | + | [[Category: Sulfolobus acidocaldarius]] |
| - | [[Category: Savvides, S N]]
| + | [[Category: De Vos D]] |
| - | [[Category: Vos, D De]] | + | [[Category: Savvides SN]] |
| - | [[Category: Allosteric]] | + | [[Category: Van Beeumen JJ]] |
| - | [[Category: Atcase]] | + | |
| - | [[Category: Ctp complex]]
| + | |
| - | [[Category: Holoenzyme]]
| + | |
| - | [[Category: Hyperthermophilic]]
| + | |
| - | [[Category: Temperature]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PYRB_SULAC
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 PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ De Vos D, Xu Y, Aerts T, Van Petegem F, Van Beeumen JJ. Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP. Biochem Biophys Res Commun. 2008 Jul 18;372(1):40-4. Epub 2008 May 12. PMID:18477471 doi:10.1016/j.bbrc.2008.04.173
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