5aga: Difference between revisions

Revision as of 04:57, 25 May 2023

Crystal structure of the Helicase domain of human DNA polymerase theta in complex with AMPPNP

Structural highlights

5aga is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ANP, FLC, K, MG
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:https://dx.doi.org/10.1016/j.str.2015.10.014

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OCA

[1] 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

[2] 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:https://dx.doi.org/10.1016/j.str.2015.10.014

[1]

[2]

@@ Line 3: / Line 3: @@
 <StructureSection load='5aga' size='340' side='right'caption='[[5aga]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5aga]] is a 1 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=5AGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AGA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5aga]] 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=5AGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AGA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5aga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aga OCA], [https://pdbe.org/5aga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aga RCSB], [https://www.ebi.ac.uk/pdbsum/5aga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aga ProSAT]</span></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=5aga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aga OCA], [http://pdbe.org/5aga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aga RCSB], [http://www.ebi.ac.uk/pdbsum/5aga PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aga 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 26: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: DNA-directed DNA polymerase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Aitkenhead, H]]
+[[Category: Aitkenhead H]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Bountra, C]]
+[[Category: Bountra C]]
-[[Category: Burgess-Brown, N]]
+[[Category: Burgess-Brown N]]
-[[Category: Cooper, C D.O]]
+[[Category: Cooper CDO]]
-[[Category: Delft, F von]]
+[[Category: Edwards A]]
-[[Category: Edwards, A]]
+[[Category: Gileadi O]]
-[[Category: Gileadi, O]]
+[[Category: Kupinska K]]
-[[Category: Kupinska, K]]
+[[Category: Newman JA]]
-[[Category: Newman, J A]]
+[[Category: Pinkas DM]]
-[[Category: Pinkas, D M]]
+[[Category: Von Delft F]]
-[[Category: Dna repair]]
-[[Category: Polq]]
-[[Category: Transferase]]

5aga: Difference between revisions

Revision as of 04:57, 25 May 2023

Crystal structure of the Helicase domain of human DNA polymerase theta in complex with AMPPNP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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