1yj5

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Revision as of 04:42, 21 November 2007

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spinqualitylabelsall models 1yj5, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Molecular architecture of mammalian polynucleotide kinase, a DNA repair enzyme

Overview

Mammalian polynucleotide kinase (PNK) is a key component of both the base, excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair, pathways. PNK acts as a 5'-kinase/3'-phosphatase to create, 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for, ligation during repair. PNK is recruited to repair complexes through, interactions between its N-terminal FHA domain and phosphorylated, components of either pathway. Here, we describe the crystal structure of, intact mammalian PNK and a structure of the PNK FHA bound to a cognate, phosphopeptide. The kinase domain has a broad substrate binding pocket, which preferentially recognizes double-stranded substrates with recessed, 5' termini. In contrast, the phosphatase domain efficiently, dephosphorylates single-stranded 3'-phospho termini as well as, double-stranded substrates. The FHA domain is linked to the, kinase/phosphatase catalytic domain by a flexible tether, and it exhibits, a mode of target selection based on electrostatic complementarity between, the binding surface and the phosphothreonine peptide.

About this Structure

1YJ5 is a Protein complex structure of sequences from Mus musculus with SO4 as ligand. Active as Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 Full crystallographic information is available from OCA.

Reference

The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase., Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JN, Mol Cell. 2005 Mar 4;17(5):657-70. PMID:15749016

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