2ihm
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(New page: 200px<br /><applet load="2ihm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ihm, resolution 2.4Å" /> '''Polymerase mu in tern...)
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Revision as of 10:12, 21 November 2007
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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 with MG, NA and D3T as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 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
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