4M04

Human DNA Polymerase Mu ternary complex

4M04 の概要

• エントリーDOI: 10.2210/pdb4m04/pdb
• 関連するPDBエントリー: 2IHM 4LZD 4LZG 4M0A
• 分子名称: DNA-directed DNA/RNA polymerase mu, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, template strand, ... (11 entities in total)
• 機能のキーワード: polymerase, dna break repair, transferase-dna complex, transferase/dna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus : Q9NP87
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46176.61

構造登録者

Moon, A.F.,Pryor, J.M.,Ramsden, D.A.,Kunkel, T.A.,Bebenek, K.,Pedersen, L.C. (登録日: 2013-08-01, 公開日: 2014-02-05, 最終更新日: 2023-09-20)

主引用文献

Moon, A.F.,Pryor, J.M.,Ramsden, D.A.,Kunkel, T.A.,Bebenek, K.,Pedersen, L.C.
Sustained active site rigidity during synthesis by human DNA polymerase mu.
Nat.Struct.Mol.Biol., 21:253-260, 2014

PubMed Abstract: DNA polymerase μ (Pol μ) is the only template-dependent human DNA polymerase capable of repairing double-strand DNA breaks (DSBs) with unpaired 3' ends in nonhomologous end joining (NHEJ). To probe this function, we structurally characterized Pol μ's catalytic cycle for single-nucleotide incorporation. These structures indicate that, unlike other template-dependent DNA polymerases, Pol μ shows no large-scale conformational changes in protein subdomains, amino acid side chains or DNA upon dNTP binding or catalysis. Instead, the only major conformational change is seen earlier in the catalytic cycle, when the flexible loop 1 region repositions upon DNA binding. Pol μ variants with changes in loop 1 have altered catalytic properties and are partially defective in NHEJ. The results indicate that specific loop 1 residues contribute to Pol μ's unique ability to catalyze template-dependent NHEJ of DSBs with unpaired 3' ends.

PubMed: 24487959
DOI: 10.1038/nsmb.2766

実験手法

X-RAY DIFFRACTION (1.898 Å)