1ot3

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[[Image:1ot3.jpg|left|200px]]
 
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==Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine==
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The line below this paragraph, containing "STRUCTURE_1ot3", creates the "Structure Box" on the page.
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<StructureSection load='1ot3' size='340' side='right'caption='[[1ot3]], [[Resolution|resolution]] 2.50&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'>[[1ot3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OT3 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]] 2.5&#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>, <scene name='pdbligand=THM:THYMIDINE'>THM</scene></td></tr>
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{{STRUCTURE_1ot3| PDB=1ot3 | 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=1ot3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ot3 OCA], [https://pdbe.org/1ot3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ot3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ot3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ot3 ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine'''
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== Function ==
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[https://www.uniprot.org/uniprot/DNK_DROME DNK_DROME] Deoxyribonucleoside kinase that has a broad specificity phosphorylating thymidine, deoxyadenosine, deoxycytidine and deoxyguanosine. Specificity is higher for pyrimidine nucleosides. Several anti-viral and anti-cancer nucleoside analogs are also efficiently phosphorylated.<ref>PMID:10446143</ref> <ref>PMID:10692477</ref> <ref>PMID:16008571</ref>
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== Evolutionary Conservation ==
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==Overview==
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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/ot/1ot3_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=1ot3 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 ==
Deoxyribonucleoside kinases are feedback inhibited by the final products of the salvage pathway, the deoxyribonucleoside triphosphates. In the present study, the mechanism of feedback inhibition is presented based on the crystal structure of a complex between the fruit fly deoxyribonucleoside kinase and its feedback inhibitor deoxythymidine triphosphate. The inhibitor was found to be bound as a bisubstrate inhibitor with its nucleoside part in the nucleoside binding site and with its phosphate groups partially occupying the phosphate donor site. The overall structure of the enzyme--inhibitor complex is very similar to the enzyme--substrate complexes with deoxythymidine and deoxycytidine, except for a conformational change within a region otherwise directly involved in catalysis. This conformational change involves a magnesium ion, which is coordinated in the inhibitor complex to the phosphates and to the primary base, Glu52, that normally is positioned close to the 5'-OH of the substrate deoxyribose.
Deoxyribonucleoside kinases are feedback inhibited by the final products of the salvage pathway, the deoxyribonucleoside triphosphates. In the present study, the mechanism of feedback inhibition is presented based on the crystal structure of a complex between the fruit fly deoxyribonucleoside kinase and its feedback inhibitor deoxythymidine triphosphate. The inhibitor was found to be bound as a bisubstrate inhibitor with its nucleoside part in the nucleoside binding site and with its phosphate groups partially occupying the phosphate donor site. The overall structure of the enzyme--inhibitor complex is very similar to the enzyme--substrate complexes with deoxythymidine and deoxycytidine, except for a conformational change within a region otherwise directly involved in catalysis. This conformational change involves a magnesium ion, which is coordinated in the inhibitor complex to the phosphates and to the primary base, Glu52, that normally is positioned close to the 5'-OH of the substrate deoxyribose.
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==About this Structure==
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Structural basis for feedback inhibition of the deoxyribonucleoside salvage pathway: studies of the Drosophila deoxyribonucleoside kinase.,Mikkelsen NE, Johansson K, Karlsson A, Knecht W, Andersen G, Piskur J, Munch-Petersen B, Eklund H Biochemistry. 2003 May 20;42(19):5706-12. PMID:12741827<ref>PMID:12741827</ref>
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1OT3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural basis for feedback inhibition of the deoxyribonucleoside salvage pathway: studies of the Drosophila deoxyribonucleoside kinase., Mikkelsen NE, Johansson K, Karlsson A, Knecht W, Andersen G, Piskur J, Munch-Petersen B, Eklund H, Biochemistry. 2003 May 20;42(19):5706-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12741827 12741827]
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</div>
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[[Category: Deoxynucleoside kinase]]
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<div class="pdbe-citations 1ot3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Andersen, G.]]
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[[Category: Andersen G]]
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[[Category: Eklund, H.]]
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[[Category: Eklund H]]
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[[Category: Johansson, K.]]
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[[Category: Johansson K]]
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[[Category: Karlsson, A.]]
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[[Category: Karlsson A]]
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[[Category: Knecht, W.]]
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[[Category: Knecht W]]
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[[Category: Mikkelsen, N E.]]
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[[Category: Mikkelsen NE]]
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[[Category: Munch-Petersen, B.]]
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[[Category: Munch-Petersen B]]
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[[Category: Piskur, J.]]
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[[Category: Piskur J]]
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[[Category: Protein-deoxynucleoside complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:15:05 2008''
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Current revision

Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine

PDB ID 1ot3

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