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| | ==Dimeric form of CTP synthase from Sulfolobus solfataricus== | | ==Dimeric form of CTP synthase from Sulfolobus solfataricus== |
| - | <StructureSection load='3nva' size='340' side='right' caption='[[3nva]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3nva' size='340' side='right'caption='[[3nva]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nva]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NVA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nva]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NVA FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyrG, SSO0201 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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]] 2.504Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/CTP_synthase_(glutamine_hydrolyzing) CTP synthase (glutamine hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.2 6.3.4.2] </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=3nva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nva OCA], [https://pdbe.org/3nva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nva RCSB], [https://www.ebi.ac.uk/pdbsum/3nva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nva ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nva OCA], [http://pdbe.org/3nva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nva RCSB], [http://www.ebi.ac.uk/pdbsum/3nva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nva ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYRG_SULSO PYRG_SULSO]] Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (By similarity). | + | [https://www.uniprot.org/uniprot/PYRG_SACS2 PYRG_SACS2] Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (PubMed:21301086). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).[HAMAP-Rule:MF_01227]<ref>PMID:21301086</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/3nva_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/3nva_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35091]] | + | [[Category: Large Structures]] |
| - | [[Category: Harris, P]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Jensen, K F]] | + | [[Category: Harris P]] |
| - | [[Category: Johansson, E]] | + | [[Category: Jensen KF]] |
| - | [[Category: Lauritsen, I]] | + | [[Category: Johansson E]] |
| - | [[Category: Willemoes, M]] | + | [[Category: Lauritsen I]] |
| - | [[Category: Ctp synthase activity]]
| + | [[Category: Willemoes M]] |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
PYRG_SACS2 Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (PubMed:21301086). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).[HAMAP-Rule:MF_01227][1]
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
CTP synthase catalyzes the last committed step in de novo pyrimidine-nucleotide biosynthesis. Active CTP synthase is a tetrameric enzyme composed of a dimer of dimers. The tetramer is favoured in the presence of the substrate nucleotides ATP and UTP; when saturated with nucleotide, the tetramer completely dominates the oligomeric state of the enzyme. Furthermore, phosphorylation has been shown to regulate the oligomeric states of the enzymes from yeast and human. The crystal structure of a dimeric form of CTP synthase from Sulfolobus solfataricus has been determined at 2.5 A resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems. Residues that are involved in the tetramerization of S. solfataricus CTP synthase according to a structural alignment with the E. coli enzyme all have large thermal parameters in the dimeric form. Furthermore, they are seen to undergo substantial movement upon tetramerization.
Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus.,Lauritsen I, Willemoes M, Jensen KF, Johansson E, Harris P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):201-8. Epub 2011 Jan 21. PMID:21301086[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lauritsen I, Willemoes M, Jensen KF, Johansson E, Harris P. Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):201-8. Epub 2011 Jan 21. PMID:21301086 doi:10.1107/S1744309110052334
- ↑ Lauritsen I, Willemoes M, Jensen KF, Johansson E, Harris P. Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):201-8. Epub 2011 Jan 21. PMID:21301086 doi:10.1107/S1744309110052334
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