1ii8
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(New page: 200px<br /><applet load="1ii8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ii8, resolution 3.02Å" /> '''Crystal structure of...)
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Revision as of 15:17, 20 November 2007
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Crystal structure of the P. furiosus Rad50 ATPase domain
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
1II8 is a Protein complex structure of sequences from Pyrococcus furiosus with PO4 as ligand. 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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