5a9j: Difference between revisions
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==Crystal structure of the Helicase domain of human DNA polymerase theta, apo-form== | ==Crystal structure of the Helicase domain of human DNA polymerase theta, apo-form== | ||
<StructureSection load='5a9j' size='340' side='right' caption='[[5a9j]], [[Resolution|resolution]] 3.55Å' scene=''> | <StructureSection load='5a9j' size='340' side='right'caption='[[5a9j]], [[Resolution|resolution]] 3.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a9j]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9J OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5a9j]] is a 4 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=5A9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9J FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.55Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9j OCA], [https://pdbe.org/5a9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9j RCSB], [https://www.ebi.ac.uk/pdbsum/5a9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DPOLQ_HUMAN DPOLQ_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.<ref>PMID:14576298</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5a9j" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5a9j" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aitkenhead | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith | [[Category: Large Structures]] | ||
[[Category: Bountra | [[Category: Aitkenhead H]] | ||
[[Category: Burgess-Brown | [[Category: Arrowsmith CH]] | ||
[[Category: Cooper | [[Category: Bountra C]] | ||
[[Category: Burgess-Brown N]] | |||
[[Category: Edwards | [[Category: Cooper CDO]] | ||
[[Category: Gileadi | [[Category: Edwards A]] | ||
[[Category: Kupinska | [[Category: Gileadi O]] | ||
[[Category: Newman | [[Category: Kupinska K]] | ||
[[Category: Pinkas | [[Category: Newman JA]] | ||
[[Category: | [[Category: Pinkas DM]] | ||
[[Category: Von Delft F]] | |||
Latest revision as of 14:06, 10 January 2024
Crystal structure of the Helicase domain of human DNA polymerase theta, apo-formCrystal structure of the Helicase domain of human DNA polymerase theta, apo-form
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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