5F3W

Structure of the ATPrS-Mre11/Rad50-DNA complex

Summary for 5F3W

• Entry DOI: 10.2210/pdb5f3w/pdb
• Descriptor: DNA double-strand break repair protein Mre11, DNA double-strand break repair Rad50 ATPase,DNA double-strand break repair Rad50 ATPase, 27-MER DNA, ... (7 entities in total)
• Functional Keywords: nuclease, complex, dna binding protein-hydrolase-dna complex, dna binding protein/hydrolase/dna
• Biological source: Methanocaldococcus jannaschii DSM 2661; More
• Total number of polymer chains: 6
• Total formula weight: 193518.56

Authors

Liu, Y. (deposition date: 2015-12-03, release date: 2016-03-02, Last modification date: 2024-03-20)

Primary citation

Liu, Y.,Sung, S.,Kim, Y.,Li, F.,Gwon, G.,Jo, A.,Kim, A.K.,Kim, T.,Song, O.K.,Lee, S.E.,Cho, Y.
ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex
Embo J., 35:743-758, 2016

PubMed Abstract: ATP-dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates repair pathway choice in cells. Here,Methanococcus jannaschii MR-ATPγS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPγS-bound Rad50 nucleotide-binding domains. Duplex DNA cannot access the Mre11 active site in the ATP-free full-length MR complex. ATP hydrolysis drives rotation of the nucleotide-binding domain and induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis-driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity.

PubMed: 26717941
DOI: 10.15252/embj.201592462

Experimental method

X-RAY DIFFRACTION (3.11 Å)