2IHM

Polymerase mu in ternary complex with gapped 11mer DNA duplex and bound incoming nucleotide

2IHM の概要

• エントリーDOI: 10.2210/pdb2ihm/pdb
• 分子名称: 5'-D(*CP*GP*GP*CP*AP*AP*TP*AP*CP*TP*G)-3', 5'-D(*CP*AP*GP*TP*AP*T)-3', 5'-D(P*GP*CP*CP*G)-3', ... (8 entities in total)
• 機能のキーワード: polymerase, helix-turn-helix, transferase-dna complex, transferase/dna
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Nucleus : Q9JIW4
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 94990.52

構造登録者

Moon, A.F.,Pedersen, L.C.,Kunkel, T.A. (登録日: 2006-09-26, 公開日: 2006-12-12, 最終更新日: 2023-09-20)

主引用文献

Moon, A.F.,Garcia-Diaz, M.,Bebenek, K.,Davis, B.J.,Zhong, X.,Ramsden, D.A.,Kunkel, T.A.,Pedersen, L.C.
Structural insight into the substrate specificity of DNA Polymerase mu.
Nat.Struct.Mol.Biol., 14:45-53, 2007

PubMed Abstract: DNA polymerase mu (Pol mu) is a family X enzyme with unique substrate specificity that contributes to its specialized role in nonhomologous DNA end joining (NHEJ). To investigate Pol mu's unusual substrate specificity, we describe the 2.4 A crystal structure of the polymerase domain of murine Pol mu bound to gapped DNA with a correct dNTP at the active site. This structure reveals substrate interactions with side chains in Pol mu that differ from other family X members. For example, a single amino acid substitution, H329A, has little effect on template-dependent synthesis by Pol mu from a paired primer terminus, but it reduces both template-independent and template-dependent synthesis during NHEJ of intermediates whose 3' ends lack complementary template strand nucleotides. These results provide insight into the substrate specificity and differing functions of four closely related mammalian family X DNA polymerases.

PubMed: 17159995
DOI: 10.1038/nsmb1180

実験手法

X-RAY DIFFRACTION (2.4 Å)