5AGA

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

5AGA の概要

• エントリーDOI: 10.2210/pdb5aga/pdb
• 分子名称: DNA POLYMERASE THETA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, CITRATE ANION, ... (6 entities in total)
• 機能のキーワード: transferase, polq, dna repair
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus : O75417
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 93959.89

構造登録者

Newman, J.A.,Cooper, C.D.O.,Aitkenhead, H.,Pinkas, D.M.,Kupinska, K.,Burgess-Brown, N.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.,Bountra, C.,Gileadi, O. (登録日: 2015-01-29, 公開日: 2015-02-25, 最終更新日: 2024-11-20)

主引用文献

Newman, J.A.,Cooper, C.D.O.,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, 23:2319-, 2015

PubMed Abstract: 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.

PubMed: 26636256
DOI: 10.1016/J.STR.2015.10.014

実験手法

X-RAY DIFFRACTION (2.9 Å)