1ii7

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Revision as of 15:17, 20 November 2007

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spinqualitylabelsall models 1ii7, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of P. furiosus Mre11 with manganese and dAMP

Overview

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.

About this Structure

1II7 is a Single protein structure of sequence from Pyrococcus furiosus with PO4, MN, SO4 and DA as ligands. Full crystallographic information is available from OCA.

Reference

Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase., Hopfner KP, Karcher A, Craig L, Woo TT, Carney JP, Tainer JA, Cell. 2001 May 18;105(4):473-85. PMID:11371344

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