3ZVL

The structural basis for substrate recognition by mammalian polynucleotide kinase 3' phosphatase

Summary for 3ZVL

• Entry DOI: 10.2210/pdb3zvl/pdb
• Related: 1UJX 1YJ5 1YJM
• Descriptor: BIFUNCTIONAL POLYNUCLEOTIDE PHOSPHATASE/KINASE, GLYCEROL, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: hydrolase-transferase complex, base excision repair, ber, non-homologous end-joining, nhej, dna repair, cancer, hydrolase/transferase
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Cellular location: Nucleus (By similarity): Q9JLV6
• Total number of polymer chains: 1
• Total formula weight: 46903.08

Authors

Garces, F.,Pearl, L.H.,Oliver, A.W. (deposition date: 2011-07-25, release date: 2011-11-16, Last modification date: 2023-12-20)

Primary citation

Garces, F.,Pearl, L.H.,Oliver, A.W.
The Structural Basis for Substrate Recognition by Mammalian Polynucleotide Kinase 3' Phosphatase.
Mol.Cell, 44:385-, 2011

PubMed Abstract: Mammalian polynucleotide kinase 3' phosphatase (PNK) plays a key role in the repair of DNA damage, functioning as part of both the nonhomologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. We have now determined crystal structures of murine PNK with DNA molecules bound to both of its active sites. The structure of ssDNA engaged with the 3'-phosphatase domain suggests a mechanism of substrate interaction that assists DNA end seeking. The structure of dsDNA bound to the 5'-kinase domain reveals a mechanism of DNA bending that facilitates recognition of DNA ends in the context of single-strand and double-strand breaks and suggests a close functional cooperation in substrate recognition between the kinase and phosphatase active sites.

PubMed: 22055185
DOI: 10.1016/J.MOLCEL.2011.08.036

Experimental method

X-RAY DIFFRACTION (1.65 Å)