2IHM

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

Summary for 2IHM

• Entry DOI: 10.2210/pdb2ihm/pdb
• Descriptor: 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)
• Functional Keywords: polymerase, helix-turn-helix, transferase-dna complex, transferase/dna
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus : Q9JIW4
• Total number of polymer chains: 8
• Total formula weight: 94990.52

Authors

Moon, A.F.,Pedersen, L.C.,Kunkel, T.A. (deposition date: 2006-09-26, release date: 2006-12-12, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)