5AGA: Crystal Structure Of The Helicase Domain Of Human Dna Polymerase Theta In Complex With Amppnp

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.
PDB ID: 5AGADownload
MMDB ID: 127366
PDB Deposition Date: 2015/1/29
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 5AGA: tetrameric; determined by author
Molecular Components in 5AGA
Label Count Molecule
Proteins (4 molecules)
DNA Polymerase Theta(Gene symbol: POLQ)
Molecule annotation
Chemicals (16 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB