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| | <StructureSection load='2uz3' size='340' side='right'caption='[[2uz3]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2uz3' size='340' side='right'caption='[[2uz3]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2uz3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27618 Atcc 27618]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xmr 1xmr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2UZ3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2uz3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ureaplasma_urealyticum Ureaplasma urealyticum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xmr 1xmr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UZ3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xmr|1xmr]], [[2b8t|2b8t]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidine_kinase Thymidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.21 2.7.1.21] </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=2uz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uz3 OCA], [https://pdbe.org/2uz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uz3 RCSB], [https://www.ebi.ac.uk/pdbsum/2uz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uz3 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2uz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uz3 OCA], [http://pdbe.org/2uz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uz3 RCSB], [http://www.ebi.ac.uk/pdbsum/2uz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uz3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KITH_UREPA KITH_UREPA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Thymidine kinase|Thymidine kinase]] | + | *[[Thymidine kinase 3D structures|Thymidine kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 27618]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thymidine kinase]] | + | [[Category: Ureaplasma urealyticum]] |
| - | [[Category: Carnrot, C]] | + | [[Category: Carnrot C]] |
| - | [[Category: Eklund, H]] | + | [[Category: Eklund H]] |
| - | [[Category: Eriksson, S]] | + | [[Category: Eriksson S]] |
| - | [[Category: Kosinska, U]] | + | [[Category: Kosinska U]] |
| - | [[Category: Mikkelsen, N E]] | + | [[Category: Mikkelsen NE]] |
| - | [[Category: Munch-Petersen, B]] | + | [[Category: Munch-Petersen B]] |
| - | [[Category: Wang, L]] | + | [[Category: Wang L]] |
| - | [[Category: Welin, M]] | + | [[Category: Welin M]] |
| - | [[Category: Zhu, C]] | + | [[Category: Zhu C]] |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Deoxyribonucleoside kinase]]
| + | |
| - | [[Category: Dna synthesis]]
| + | |
| - | [[Category: Dttp]]
| + | |
| - | [[Category: Feed-back inhibitor]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Lasso-domain]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Tk1]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Uu-tk]]
| + | |
| - | [[Category: Zinc-binding domain]]
| + | |
| Structural highlights
Function
KITH_UREPA
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
Cytosolic thymidine kinase 1, TK1, is a well known cell-cycle-regulated enzyme of importance in nucleotide metabolism as well as an activator of antiviral and anticancer drugs such as 3'-azido-3'-deoxythymidine (AZT). We have now determined the structures of the TK1 family, the human and Ureaplasma urealyticum enzymes, in complex with the feedback inhibitor dTTP. The TK1s have a tetrameric structure in which each subunit contains an alpha/beta-domain that is similar to ATPase domains of members of the RecA structural family and a domain containing a structural zinc. The zinc ion connects beta-structures at the root of a beta-ribbon that forms a stem that widens to a lasso-type loop. The thymidine of dTTP is hydrogen-bonded to main-chain atoms predominantly coming from the lasso loop. This binding is in contrast to other deoxyribonucleoside kinases where specific interactions occur with side chains. The TK1 structure differs fundamentally from the structures of the other deoxyribonucleoside kinases, indicating a different evolutionary origin.
Structures of thymidine kinase 1 of human and mycoplasmic origin.,Welin M, Kosinska U, Mikkelsen NE, Carnrot C, Zhu C, Wang L, Eriksson S, Munch-Petersen B, Eklund H Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17970-5. Epub 2004 Dec 20. PMID:15611477[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Welin M, Kosinska U, Mikkelsen NE, Carnrot C, Zhu C, Wang L, Eriksson S, Munch-Petersen B, Eklund H. Structures of thymidine kinase 1 of human and mycoplasmic origin. Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17970-5. Epub 2004 Dec 20. PMID:15611477
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