1tev

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[[Image:1tev.jpg|left|200px]]
 
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==Crystal structure of the human UMP/CMP kinase in open conformation==
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The line below this paragraph, containing "STRUCTURE_1tev", creates the "Structure Box" on the page.
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<StructureSection load='1tev' size='340' side='right'caption='[[1tev]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1tev]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEV FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.1&#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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{{STRUCTURE_1tev| PDB=1tev | SCENE= }}
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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=1tev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tev OCA], [https://pdbe.org/1tev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tev RCSB], [https://www.ebi.ac.uk/pdbsum/1tev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tev ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KCY_HUMAN KCY_HUMAN] Catalyzes specific phosphoryl transfer from ATP to UMP and CMP.
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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/te/1tev_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=1tev 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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Human UMP/CMP kinase plays a crucial role in supplying precursors for nucleic acid synthesis by catalyzing the conversion of UMP, CMP, and dCMP into their diphosphate form. In addition, this kinase is an essential component of the activation cascade of medicinally relevant nucleoside analog prodrugs such as AraC, gemcitabine, and ddC. During the catalytic cycle the enzyme undergoes large conformational changes from open in the absence of substrates to closed in the presence of both phosphoryl donor and phosphoryl acceptor. Here we report the crystal structure of the substrate-free, open form of human UMP/CMP kinase. Comparison of the open structure with the closed state previously reported for the similar Dictyostelium discoideum UMP/CMP kinase reveals the conformational changes that occur upon substrate binding. We observe a classic example of induced fit where substrate-induced conformational changes in hinge residues result in rigid body movements of functional domains to form the catalytically competent state. In addition, a homology model of the human enzyme in the closed state based on the structure of D. discoideum UMP/CMP kinase aids to rationalize the substrate specificity of the human enzyme.
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'''Crystal structure of the human UMP/CMP kinase in open conformation'''
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Substrate-induced conformational changes in human UMP/CMP kinase.,Segura-Pena D, Sekulic N, Ort S, Konrad M, Lavie A J Biol Chem. 2004 Aug 6;279(32):33882-9. Epub 2004 May 26. PMID:15163660<ref>PMID:15163660</ref>
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==Overview==
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Human UMP/CMP kinase plays a crucial role in supplying precursors for nucleic acid synthesis by catalyzing the conversion of UMP, CMP, and dCMP into their diphosphate form. In addition, this kinase is an essential component of the activation cascade of medicinally relevant nucleoside analog prodrugs such as AraC, gemcitabine, and ddC. During the catalytic cycle the enzyme undergoes large conformational changes from open in the absence of substrates to closed in the presence of both phosphoryl donor and phosphoryl acceptor. Here we report the crystal structure of the substrate-free, open form of human UMP/CMP kinase. Comparison of the open structure with the closed state previously reported for the similar Dictyostelium discoideum UMP/CMP kinase reveals the conformational changes that occur upon substrate binding. We observe a classic example of induced fit where substrate-induced conformational changes in hinge residues result in rigid body movements of functional domains to form the catalytically competent state. In addition, a homology model of the human enzyme in the closed state based on the structure of D. discoideum UMP/CMP kinase aids to rationalize the substrate specificity of the human enzyme.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1TEV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEV OCA].
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</div>
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<div class="pdbe-citations 1tev" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Substrate-induced conformational changes in human UMP/CMP kinase., Segura-Pena D, Sekulic N, Ort S, Konrad M, Lavie A, J Biol Chem. 2004 Aug 6;279(32):33882-9. Epub 2004 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15163660 15163660]
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*[[Cytidine monophosphate kinase|Cytidine monophosphate kinase]]
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[[Category: Cytidylate kinase]]
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*[[UMP/CMP kinase|UMP/CMP kinase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Konrad, M.]]
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[[Category: Konrad M]]
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[[Category: Lavie, A.]]
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[[Category: Lavie A]]
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[[Category: Ort, S.]]
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[[Category: Ort S]]
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[[Category: Segura-Pena, D.]]
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[[Category: Segura-Pena D]]
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[[Category: Sekulic, N.]]
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[[Category: Sekulic N]]
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[[Category: Conformational change]]
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[[Category: Kinase]]
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[[Category: Lid region]]
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[[Category: Nmp binding region]]
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[[Category: Ploop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:51:55 2008''
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Current revision

Crystal structure of the human UMP/CMP kinase in open conformation

PDB ID 1tev

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