5a9j

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the Helicase domain of human DNA polymerase theta, apo-form

Structural highlights

5a9j is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.55Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

Publication Abstract from PubMed

DNA 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.

References

↑ Seki M, Marini F, Wood RD. POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003 Nov 1;31(21):6117-26. PMID:14576298
↑ Newman JA, Cooper CD, Aitkenhead H, Gileadi O. Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway. Structure. 2015 Dec 1;23(12):2319-30. doi: 10.1016/j.str.2015.10.014. PMID:26636256 doi:http://dx.doi.org/10.1016/j.str.2015.10.014

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5a9j"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Helicase domain of human DNA polymerase theta, apo-form==
-<StructureSection load='5a9j' size='340' side='right' caption='[[5a9j]], [[Resolution|resolution]] 3.55&Aring;' scene=''>
+<StructureSection load='5a9j' size='340' side='right'caption='[[5a9j]], [[Resolution|resolution]] 3.55&Aring;' scene=''>
 == 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A9J FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a9f|5a9f]]</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]] 3.55&#8491;</td></tr>
-<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=5a9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9j OCA], [http://pdbe.org/5a9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a9j RCSB], [http://www.ebi.ac.uk/pdbsum/5a9j PDBsum]</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=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>
 == Function ==
-[[http://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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5a9j" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aitkenhead, H]]
+[[Category: Homo sapiens]]
-[[Category: Arrowsmith, C H]]
+[[Category: Large Structures]]
-[[Category: Bountra, C]]
+[[Category: Aitkenhead H]]
-[[Category: Burgess-Brown, N]]
+[[Category: Arrowsmith CH]]
-[[Category: Cooper, C D.O]]
+[[Category: Bountra C]]
-[[Category: Delft, F von]]
+[[Category: Burgess-Brown N]]
-[[Category: Edwards, A]]
+[[Category: Cooper CDO]]
-[[Category: Gileadi, O]]
+[[Category: Edwards A]]
-[[Category: Kupinska, K]]
+[[Category: Gileadi O]]
-[[Category: Newman, J A]]
+[[Category: Kupinska K]]
-[[Category: Pinkas, D M]]
+[[Category: Newman JA]]
-[[Category: Dna repair]]
+[[Category: Pinkas DM]]
-[[Category: Helicase]]
+[[Category: Von Delft F]]
-[[Category: Hydrolase]]
-[[Category: Polq]]
-[[Category: Polymerase]]

5a9j

From Proteopedia

Current revision

Crystal structure of the Helicase domain of human DNA polymerase theta, apo-form

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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