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1YJ5

Molecular architecture of mammalian polynucleotide kinase, a DNA repair enzyme

Summary for 1YJ5
Entry DOI10.2210/pdb1yj5/pdb
Descriptor5' polynucleotide kinase-3' phosphatase catalytic domain, 5' polynucleotide kinase-3' phosphatase FHA domain, SULFATE ION, ... (4 entities in total)
Functional Keywordsbeta sandwich, p-loop, transferase
Biological sourceMus musculus (house mouse)
More
Cellular locationNucleus (By similarity): Q9JLV6 Q9JLV6
Total number of polymer chains3
Total formula weight101849.08
Authors
Primary citationBernstein, 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: 15749016
DOI: 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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数据于2024-11-06公开中

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