4TMU

Crystal structure of RecQ catalytic core from C. sakazakii bound to DNA

4TMU の概要

• エントリーDOI: 10.2210/pdb4tmu/pdb
• 分子名称: RecQ, DNA (29-MER), ZINC ION, ... (4 entities in total)
• 機能のキーワード: recq, helicase, winged helix, atp binding, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Cronobacter sakazakii; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70959.40

構造登録者

Manthei, K.A.,Keck, J.L. (登録日: 2014-06-02, 公開日: 2015-03-11, 最終更新日: 2023-12-27)

主引用文献

Manthei, K.A.,Hill, M.C.,Burke, J.E.,Butcher, S.E.,Keck, J.L.
Structural mechanisms of DNA binding and unwinding in bacterial RecQ helicases.
Proc.Natl.Acad.Sci.USA, 112:4292-4297, 2015

PubMed Abstract: RecQ helicases unwind remarkably diverse DNA structures as key components of many cellular processes. How RecQ enzymes accommodate different substrates in a unified mechanism that couples ATP hydrolysis to DNA unwinding is unknown. Here, the X-ray crystal structure of the Cronobacter sakazakii RecQ catalytic core domain bound to duplex DNA with a 3' single-stranded extension identifies two DNA-dependent conformational rearrangements: a winged-helix domain pivots ∼90° to close onto duplex DNA, and a conserved aromatic-rich loop is remodeled to bind ssDNA. These changes coincide with a restructuring of the RecQ ATPase active site that positions catalytic residues for ATP hydrolysis. Complex formation also induces a tight bend in the DNA and melts a portion of the duplex. This bending, coupled with translocation, could provide RecQ with a mechanism for unwinding duplex and other DNA structures.

PubMed: 25831501
DOI: 10.1073/pnas.1416746112

実験手法

X-RAY DIFFRACTION (2.4 Å)