8EFK

Structure of Lates calcarifer DNA polymerase theta polymerase domain with hairpin DNA

8EFK の概要

• エントリーDOI: 10.2210/pdb8efk/pdb
• EMDBエントリー: 28084
• 分子名称: Lates calcarifer DNA polymerase theta, DNA (5'-D(P*TP*TP*TP*TP*GP*GP*CP*TP*TP*TP*TP*GP*CP*CP*(2DA))-3'), MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: dna double-strand break repair, microhomology-mediated end joining, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Lates calcarifer; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103452.29

構造登録者

Li, C.,Zhu, H.,Sun, J.,Gao, Y. (登録日: 2022-09-08, 公開日: 2022-12-14, 最終更新日: 2025-06-04)

主引用文献

Li, C.,Zhu, H.,Jin, S.,Maksoud, L.M.,Jain, N.,Sun, J.,Gao, Y.
Structural basis of DNA polymerase theta mediated DNA end joining.
Nucleic Acids Res., 51:463-474, 2023

PubMed Abstract: DNA polymerase θ (Pol θ) plays an essential role in the microhomology-mediated end joining (MMEJ) pathway for repairing DNA double-strand breaks. However, the mechanisms by which Pol θ recognizes microhomologous DNA ends and performs low-fidelity DNA synthesis remain unclear. Here, we present cryo-electron microscope structures of the polymerase domain of Lates calcarifer Pol θ with long and short duplex DNA at up to 2.4 Å resolution. Interestingly, Pol θ binds to long and short DNA substrates similarly, with extensive interactions around the active site. Moreover, Pol θ shares a similar active site as high-fidelity A-family polymerases with its finger domain well-closed but differs in having hydrophilic residues surrounding the nascent base pair. Computational simulations and mutagenesis studies suggest that the unique insertion loops of Pol θ help to stabilize short DNA binding and assemble the active site for MMEJ repair. Taken together, our results illustrate the structural basis of Pol θ-mediated MMEJ.

PubMed: 36583344
DOI: 10.1093/nar/gkac1201

実験手法

ELECTRON MICROSCOPY (3 Å)