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PDBsum entry 5a9f
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PDB id:
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Transferase
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Title:
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Crystal structure of the helicase domain of human DNA polymerase theta in complex with adp
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Structure:
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DNA polymerase theta. Chain: a. Fragment: helicase domain, residues 67-894. Synonym: DNA polymerase eta. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
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Resolution:
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3.20Å
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R-factor:
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0.229
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R-free:
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0.273
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Authors:
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J.A.Newman,C.D.O.Cooper,H.Aitkenhead,D.M.Pinkas,K.Kupinska,N.Burgess- Brown,F.Von Delft,C.H.Arrowsmith,A.Edwards,C.Bountra,O.Gileadi
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Key ref:
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J.A.Newman
et al.
(2015).
Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway.
Structure,
23,
2319-2330.
PubMed id:
DOI:
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Date:
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21-Jul-15
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Release date:
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16-Dec-15
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PROCHECK
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Headers
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References
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O75417
(DPOLQ_HUMAN) -
DNA polymerase theta from Homo sapiens
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Seq:
Struc:
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2590 a.a.
780 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class 2:
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E.C.2.7.7.49
- RNA-directed Dna polymerase.
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Reaction:
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
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DNA(n)
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+
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2'-deoxyribonucleoside 5'-triphosphate
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=
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DNA(n+1)
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+
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diphosphate
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Enzyme class 3:
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E.C.2.7.7.7
- DNA-directed Dna polymerase.
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Reaction:
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
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DNA(n)
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+
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2'-deoxyribonucleoside 5'-triphosphate
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=
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DNA(n+1)
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+
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diphosphate
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Enzyme class 4:
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E.C.3.6.4.12
- Dna helicase.
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Reaction:
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ATP + H2O = ADP + phosphate + H+
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ATP
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+
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H2O
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=
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ADP
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+
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phosphate
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Structure
23:2319-2330
(2015)
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PubMed id:
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Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway.
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J.A.Newman,
C.D.Cooper,
H.Aitkenhead,
O.Gileadi.
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ABSTRACT
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DNA polymerase theta (Polθ) has been identified as a crucial alternative
non-homologous end-joining factor in mammalian cells. Polθ 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 Polθ 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. Polθ exists as a tetramer both in the crystals and in
solution. We propose a model for DNA binding to the Polθ helicase domain in the
context of the Polθ tetramer, which suggests a role for the helicase domain in
strand annealing of DNA templates for subsequent processing by the polymerase
domain.
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Links
