1YJ5
Molecular architecture of mammalian polynucleotide kinase, a DNA repair enzyme
Summary for 1YJ5
Entry DOI | 10.2210/pdb1yj5/pdb |
Descriptor | 5' polynucleotide kinase-3' phosphatase catalytic domain, 5' polynucleotide kinase-3' phosphatase FHA domain, SULFATE ION, ... (4 entities in total) |
Functional Keywords | beta sandwich, p-loop, transferase |
Biological source | Mus musculus (house mouse) More |
Cellular location | Nucleus (By similarity): Q9JLV6 Q9JLV6 |
Total number of polymer chains | 3 |
Total formula weight | 101849.08 |
Authors | Bernstein, N.K.,Williams, R.S.,Rakovszky, M.L.,Cui, D.,Green, R.,Karimi-Busheri, F.,Mani, R.S.,Galicia, S.,Koch, C.A.,Cass, C.E.,Durocher, D.,Weinfeld, M.,Glover, J.N.M. (deposition date: 2005-01-13, release date: 2005-03-15, Last modification date: 2024-10-30) |
Primary citation | Bernstein, N.K.,Williams, R.S.,Rakovszky, M.L.,Cui, D.,Green, R.,Karimi-Busheri, F.,Mani, R.S.,Galicia, S.,Koch, C.A.,Cass, C.E.,Durocher, D.,Weinfeld, M.,Glover, J.N. The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase. Mol.Cell, 17:657-670, 2005 Cited by PubMed Abstract: 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. PubMed: 15749016DOI: 10.1016/j.molcel.2005.02.012 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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