5a9f: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a9f]] 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=5A9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9F FirstGlance]. <br> | <table><tr><td colspan='2'>[[5a9f]] 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=5A9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 3.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5a9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9f OCA], [https://pdbe.org/5a9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9f RCSB], [https://www.ebi.ac.uk/pdbsum/5a9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9f ProSAT]</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=5a9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9f OCA], [https://pdbe.org/5a9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9f RCSB], [https://www.ebi.ac.uk/pdbsum/5a9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 14:06, 10 January 2024
Crystal structure of the Helicase domain of human DNA polymerase theta in complex with ADPCrystal structure of the Helicase domain of human DNA polymerase theta in complex with ADP
Structural highlights
FunctionDPOLQ_HUMAN Has a DNA polymerase activity on nicked double-stranded DNA and on a singly primed DNA template. The enzyme activity is resistant to aphidicolin, and inhibited by dideoxynucleotides. Exhibites a single-stranded DNA-dependent ATPase activity. Could be involved in the repair of interstrand cross-links.[1] Publication Abstract from PubMedDNA polymerase theta (Poltheta) has been identified as a crucial alternative non-homologous end-joining factor in mammalian cells. Poltheta is upregulated in a range of cancer cell types defective in homologous recombination, and knockdown has been shown to inhibit cell survival in a subset of these, making it an attractive target for cancer treatment. We present crystal structures of the helicase domain of human Poltheta in the presence and absence of bound nucleotides, and a characterization of its DNA-binding and DNA-stimulated ATPase activities. Comparisons with related helicases from the Hel308 family identify several unique features. Poltheta exists as a tetramer both in the crystals and in solution. We propose a model for DNA binding to the Poltheta helicase domain in the context of the Poltheta tetramer, which suggests a role for the helicase domain in strand annealing of DNA templates for subsequent processing by the polymerase domain. Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway.,Newman JA, Cooper CD, Aitkenhead H, Gileadi O Structure. 2015 Dec 1;23(12):2319-30. doi: 10.1016/j.str.2015.10.014. PMID:26636256[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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