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| | ==Crystal Structure of T.th. HB8 CTP synthetase== | | ==Crystal Structure of T.th. HB8 CTP synthetase== |
| - | <StructureSection load='1vcm' size='340' side='right' caption='[[1vcm]], [[Resolution|resolution]] 2.35Å' scene=''> | + | <StructureSection load='1vcm' size='340' side='right'caption='[[1vcm]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1vcm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VCM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1vcm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VCM FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vcn|1vcn]], [[1vco|1vco]]</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]] 2.35Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HB8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</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=1vcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcm OCA], [https://pdbe.org/1vcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vcm RCSB], [https://www.ebi.ac.uk/pdbsum/1vcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcm ProSAT], [https://www.topsan.org/Proteins/RSGI/1vcm TOPSAN]</span></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>
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| - | <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=1vcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcm OCA], [http://pdbe.org/1vcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vcm RCSB], [http://www.ebi.ac.uk/pdbsum/1vcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcm ProSAT], [http://www.topsan.org/Proteins/RSGI/1vcm TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYRG_THET8 PYRG_THET8]] 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_THET8 PYRG_THET8] Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (By similarity). |
| | == 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: Flavobacterium thermophilum yoshida and oshima 1971]] | + | [[Category: Large Structures]] |
| - | [[Category: Goto, M]] | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Structural genomic]] | + | [[Category: Goto M]] |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Tetramer]]
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| Structural highlights
Function
PYRG_THET8 Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (By similarity).
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 synthetase (CTPs) catalyzes the last step in CTP biosynthesis, in which ammonia generated at the glutaminase domain reacts with the ATP-phosphorylated UTP at the synthetase domain to give CTP. Glutamine hydrolysis is active in the presence of ATP and UTP and is stimulated by the addition of GTP. We report the crystal structures of Thermus thermophilus HB8 CTPs alone, CTPs with 3SO4(2-), and CTPs with glutamine. The enzyme is folded into a homotetramer with a cross-shaped structure. Based on the binding mode of sulfate anions to the synthetase site, ATP and UTP are computer modeled into CTPs with a geometry favorable for the reaction. Glutamine bound to the glutaminase domain is situated next to the triad of Glu-His-Cys as a catalyst and a water molecule. Structural information provides an insight into the conformational changes associated with the binding of ATP and UTP and the formation of the GTP binding site.
Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites.,Goto M, Omi R, Nakagawa N, Miyahara I, Hirotsu K Structure. 2004 Aug;12(8):1413-23. PMID:15296735[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goto M, Omi R, Nakagawa N, Miyahara I, Hirotsu K. Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites. Structure. 2004 Aug;12(8):1413-23. PMID:15296735 doi:http://dx.doi.org/10.1016/j.str.2004.05.013
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