2ihm
From Proteopedia
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| , resolution 2.4Å | |||||||
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| Ligands: | , , , , , , | ||||||
| Gene: | Polm (Mus musculus) | ||||||
| Activity: | DNA-directed DNA polymerase, with EC number 2.7.7.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Polymerase mu in ternary complex with gapped 11mer DNA duplex and bound incoming nucleotide
Overview
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.
About this Structure
2IHM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural insight into the substrate specificity of DNA Polymerase mu., Moon AF, Garcia-Diaz M, Bebenek K, Davis BJ, Zhong X, Ramsden DA, Kunkel TA, Pedersen LC, Nat Struct Mol Biol. 2007 Jan;14(1):45-53. Epub 2006 Dec 10. PMID:17159995
Page seeded by OCA on Mon Mar 31 03:44:27 2008
