3ZVM

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

3ZVM の概要

• エントリーDOI: 10.2210/pdb3zvm/pdb
• 関連するPDBエントリー: 1UJX 1YJ5 1YJM 3ZVL 3ZVN
• 分子名称: BIFUNCTIONAL POLYNUCLEOTIDE PHOSPHATASE/KINASE, 5'-D(*GP*TP*CP*AP*CP)-3', ADENOSINE-5'-DIPHOSPHATE, ... (8 entities in total)
• 機能のキーワード: hydrolase-transferase-dna complex, base excision repair, ber, non-homologous end-joining, nhej, dna repair, cancer, hydrolase/transferase/dna
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Nucleus : Q9JLV6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 97107.55

構造登録者

Garces, F.,Pearl, L.H.,Oliver, A.W. (登録日: 2011-07-25, 公開日: 2011-11-16, 最終更新日: 2023-12-20)

主引用文献

Garces, F.,Pearl, L.H.,Oliver, A.W.
The structural basis for substrate recognition by mammalian polynucleotide kinase 3' phosphatase.
Mol. Cell, 44:385-396, 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

実験手法

X-RAY DIFFRACTION (1.997 Å)