1II8

Crystal structure of the P. furiosus Rad50 ATPase domain

Summary for 1II8

• Entry DOI: 10.2210/pdb1ii8/pdb
• Related: 1F2T 1F2U 1II7
• Descriptor: Rad50 ABC-ATPase, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: rad50, mre11, dna double-strand break repair, atp, replication
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 2
• Total formula weight: 42843.39

Authors

Hopfner, K.-P.,Karcher, A.,Craig, L.,Woo, T.T.,Carney, J.P.,Tainer, J.A. (deposition date: 2001-04-20, release date: 2001-05-30, Last modification date: 2023-08-16)

Primary citation

Hopfner, K.P.,Karcher, A.,Craig, L.,Woo, T.T.,Carney, J.P.,Tainer, J.A.
Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase.
Cell(Cambridge,Mass.), 105:473-485, 2001

PubMed Abstract: To clarify functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair, we report Pyrococcus furiosus Mre11 crystal structures, revealing a protein phosphatase-like, dimanganese binding domain capped by a unique domain controlling active site access. These structures unify Mre11's multiple nuclease activities in a single endo/exonuclease mechanism and reveal eukaryotic macromolecular interaction sites by mapping human and yeast Mre11 mutations. Furthermore, the structure of the P. furiosus Rad50 ABC-ATPase with its adjacent coiled-coil defines a compact Mre11/Rad50-ATPase complex and suggests that Rad50-ATP-driven conformational switching directly controls the Mre11 exonuclease. Electron microscopy, small angle X-ray scattering, and ultracentrifugation data of human and P. furiosus MR reveal a dual functional complex consisting of a (Mre11)2/(Rad50)2 heterotetrameric DNA processing head and a double coiled-coil linker.

PubMed: 11371344
DOI: 10.1016/S0092-8674(01)00335-X

Experimental method

X-RAY DIFFRACTION (3.02 Å)