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| ==Human DNA polymerase kappa extending opposite a cis-syn thymine dimer== | | ==Human DNA polymerase kappa extending opposite a cis-syn thymine dimer== |
| <StructureSection load='3pzp' size='340' side='right' caption='[[3pzp]], [[Resolution|resolution]] 3.34Å' scene=''> | | <StructureSection load='3pzp' size='340' side='right'caption='[[3pzp]], [[Resolution|resolution]] 3.34Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3pzp]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PZP FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3pzp]] is a 6 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=3PZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZP FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.336Å</td></tr> |
| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TTD:CIS-SYN+CYCLOBUTANE+THYMINE+DIMER'>TTD</scene></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTD:CIS-SYN+CYCLOBUTANE+THYMINE+DIMER'>TTD</scene></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t94|1t94]], [[2oh2|2oh2]], [[3in5|3in5]]</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=3pzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzp OCA], [https://pdbe.org/3pzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzp RCSB], [https://www.ebi.ac.uk/pdbsum/3pzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzp ProSAT]</span></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">POLK, DINB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=3pzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzp OCA], [http://pdbe.org/3pzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pzp RCSB], [http://www.ebi.ac.uk/pdbsum/3pzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzp ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/POLK_HUMAN POLK_HUMAN]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.<ref>PMID:10620008</ref> <ref>PMID:11024016</ref> <ref>PMID:12145297</ref> <ref>PMID:12444249</ref> <ref>PMID:12952891</ref> <ref>PMID:14630940</ref> <ref>PMID:15533436</ref> | | [https://www.uniprot.org/uniprot/POLK_HUMAN POLK_HUMAN] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.<ref>PMID:10620008</ref> <ref>PMID:11024016</ref> <ref>PMID:12145297</ref> <ref>PMID:12444249</ref> <ref>PMID:12952891</ref> <ref>PMID:14630940</ref> <ref>PMID:15533436</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Exposure of DNA to UV radiation causes covalent linkages between adjacent pyrimidines. The most common lesion found in DNA from these UV-induced linkages is the cis-syn cyclobutane pyrimidine dimer. Human DNA polymerase kappa (Polkappa), a member of the Y-family of DNA polymerases, is unable to insert nucleotides opposite the 3'T of a cis-syn T-T dimer, but it can efficiently extend from a nucleotide inserted opposite the 3'T of the dimer by another DNA polymerase. We present here the structure of human Polkappa in the act of inserting a nucleotide opposite the 5'T of the cis-syn T-T dimer. The structure reveals a constrained active-site cleft that is unable to accommodate the 3'T of a cis-syn T-T dimer but is remarkably well adapted to accommodate the 5'T via Watson-Crick base pairing, in accord with a proposed role for Polkappa in the extension reaction opposite from cyclobutane pyrimidine dimers in vivo.
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| Role of human DNA polymerase kappa in extension opposite from a cis-syn thymine dimer.,Vasquez-Del Carpio R, Silverstein TD, Lone S, Johnson RE, Prakash L, Prakash S, Aggarwal AK J Mol Biol. 2011 Apr 29;408(2):252-61. Epub 2011 Feb 24. PMID:21354175<ref>PMID:21354175</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3pzp" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[DNA polymerase|DNA polymerase]] | | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: DNA-directed DNA polymerase]] | | [[Category: Homo sapiens]] |
| [[Category: Human]] | | [[Category: Large Structures]] |
| [[Category: Aggarwal, A K]] | | [[Category: Aggarwal AK]] |
| [[Category: Carpio, R Vasquez-Del]]
| | [[Category: Johnson RE]] |
| [[Category: Johnson, R E]] | | [[Category: Lone S]] |
| [[Category: Lone, S]] | | [[Category: Prakash L]] |
| [[Category: Prakash, L]] | | [[Category: Prakash S]] |
| [[Category: Prakash, S]] | | [[Category: Silverstein TD]] |
| [[Category: Silverstein, T D]] | | [[Category: Vasquez-Del Carpio R]] |
| [[Category: Dna binding nucleotide binding magnesium binding]] | |
| [[Category: Dna nucleotidyltransferase]]
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| [[Category: Nucleus]]
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| [[Category: Transferase-dna complex]]
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