2vo1

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[[Image:2vo1.png|left|200px]]
 
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{{STRUCTURE_2vo1| PDB=2vo1 | SCENE= }}
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==CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE==
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<StructureSection load='2vo1' size='340' side='right'caption='[[2vo1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vo1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2c5m 2c5m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VO1 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]] 2.8&#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=SO4:SULFATE+ION'>SO4</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=2vo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vo1 OCA], [https://pdbe.org/2vo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vo1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vo1 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PYRG1_HUMAN PYRG1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. A unique and recessive G to C mutation probably affecting a splice donor site at the junction of intron 17-18 and exon 18 has been identified in all patients. It results in expression of an abnormal transcript lacking exon 18 and a complete loss of the expression of the protein.<ref>PMID:24870241</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRG1_HUMAN PYRG1_HUMAN] This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity.<ref>PMID:16179339</ref> <ref>PMID:24870241</ref>
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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/vo/2vo1_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=2vo1 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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Cytidine triphosphate synthetase (CTPS) is a key enzyme in nucleic acid and phospholipid biosynthesis and its activity is increased in certain human cancers, making it a promising drug target. The crystal structure of the synthetase domain of human CTPS, which represents the first structure of a CTPS from an eukaryote, has been determined. The structure is homotetrameric and each active site is formed by three different subunits. Sulfate ions bound to the active sites indicate the positions of phosphate-binding sites for the substrates ATP and UTP and the feedback inhibitor CTP. Together with earlier structures of bacterial CTPS, the human CTPS structure provides an extended understanding of the structure-function relationship of CTPS-family members. The structure also serves as a basis for structure-based design of anti-proliferative inhibitors.
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===CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE===
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Structure of the synthetase domain of human CTP synthetase, a target for anticancer therapy.,Kursula P, Flodin S, Ehn M, Hammarstrom M, Schuler H, Nordlund P, Stenmark P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt, 7):613-7. Epub 2006 Jun 10. PMID:16820675<ref>PMID:16820675</ref>
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{{ABSTRACT_PUBMED_16820675}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2vo1" style="background-color:#fffaf0;"></div>
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[[2vo1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2c5m 2c5m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VO1 OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016820675</ref><references group="xtra"/>
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</StructureSection>
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[[Category: CTP synthase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C.]]
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[[Category: Large Structures]]
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[[Category: Berg, S Van Den.]]
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[[Category: Arrowsmith C]]
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[[Category: Berglund, H.]]
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[[Category: Berglund H]]
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[[Category: Edwards, A.]]
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[[Category: Edwards A]]
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[[Category: Ehn, M.]]
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[[Category: Ehn M]]
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[[Category: Flodin, S.]]
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[[Category: Flodin S]]
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[[Category: Graslund, S.]]
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[[Category: Graslund S]]
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[[Category: Hallberg, B M.]]
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[[Category: Hallberg BM]]
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[[Category: Hammarstrom, M.]]
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[[Category: Hammarstrom M]]
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[[Category: Holmberg-Schiavone, L.]]
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[[Category: Holmberg-Schiavone L]]
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[[Category: Kotenyoa, T.]]
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[[Category: Kotenyoa T]]
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[[Category: Kursula, P.]]
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[[Category: Kursula P]]
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[[Category: Moche, M.]]
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[[Category: Moche M]]
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[[Category: Nilsson-Ehle, P.]]
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[[Category: Nilsson-Ehle P]]
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[[Category: Nordlund, P.]]
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[[Category: Nordlund P]]
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[[Category: Ogg, D.]]
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[[Category: Ogg D]]
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[[Category: Persson, C.]]
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[[Category: Persson C]]
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[[Category: Sagemark, J.]]
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[[Category: Sagemark J]]
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[[Category: Schuler, H.]]
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[[Category: Schuler H]]
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[[Category: Stenmark, P.]]
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[[Category: Stenmark P]]
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[[Category: Sundstrom, M.]]
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[[Category: Sundstrom M]]
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[[Category: Thorsell, A G.]]
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[[Category: Thorsell AG]]
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[[Category: Weigelt, J.]]
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[[Category: Van Den Berg S]]
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[[Category: Amidotransferase]]
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[[Category: Weigelt J]]
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[[Category: Ctp]]
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[[Category: Ctp synthase]]
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[[Category: Ctp synthetase]]
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[[Category: Ctp]]
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[[Category: Cytidine 5-prime triphosphate synthetase]]
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[[Category: Glutamine]]
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[[Category: Glutamine amidotransferase]]
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[[Category: Ligase]]
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[[Category: Phosphoprotein]]
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[[Category: Phosphorylation]]
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[[Category: Pyrimidine biosynthesis]]
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[[Category: Utp]]
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Current revision

CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE

PDB ID 2vo1

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