1F2U

Crystal Structure of RAD50 ABC-ATPase

1F2U の概要

• エントリーDOI: 10.2210/pdb1f2u/pdb
• 関連するPDBエントリー: 1F2T
• 分子名称: RAD50 ABC-ATPASE, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: dna double-strand break repair, abc-atpase, replication
• 由来する生物種: Pyrococcus furiosus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68859.51

構造登録者

Hopfner, K.P.,Karcher, A.,Shin, D.S.,Craig, L. (登録日: 2000-05-29, 公開日: 2000-08-02, 最終更新日: 2024-02-07)

主引用文献

Hopfner, K.P.,Karcher, A.,Shin, D.S.,Craig, L.,Arthur, L.M.,Carney, J.P.,Tainer, J.A.
Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily.
Cell(Cambridge,Mass.), 101:789-800, 2000

PubMed Abstract: To clarify the key role of Rad50 in DNA double-strand break repair (DSBR), we biochemically and structurally characterized ATP-bound and ATP-free Rad50 catalytic domain (Rad50cd) from Pyrococcus furiosus. Rad50cd displays ATPase activity plus ATP-controlled dimerization and DNA binding activities. Rad50cd crystal structures identify probable protein and DNA interfaces and reveal an ABC-ATPase fold, linking Rad50 molecular mechanisms to ABC transporters, including P glycoprotein and cystic fibrosis transmembrane conductance regulator. Binding of ATP gamma-phosphates to conserved signature motifs in two opposing Rad50cd molecules promotes dimerization that likely couples ATP hydrolysis to dimer dissociation and DNA release. These results, validated by mutations, suggest unified molecular mechanisms for ATP-driven cooperativity and allosteric control of ABC-ATPases in DSBR, membrane transport, and chromosome condensation by SMC proteins.

PubMed: 10892749
DOI: 10.1016/S0092-8674(00)80890-9

実験手法

X-RAY DIFFRACTION (1.6 Å)