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1ii7

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[[Image:1ii7.gif|left|200px]]
[[Image:1ii7.gif|left|200px]]
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{{Structure
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|PDB= 1ii7 |SIZE=350|CAPTION= <scene name='initialview01'>1ii7</scene>, resolution 2.20&Aring;
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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{{STRUCTURE_1ii7| PDB=1ii7 | SCENE= }}
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|RELATEDENTRY=[[1ii8|1II8]], [[1f2t|1F2T]], [[1f2u|1F2U]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ii7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii7 OCA], [http://www.ebi.ac.uk/pdbsum/1ii7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ii7 RCSB]</span>
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'''Crystal structure of P. furiosus Mre11 with manganese and dAMP'''
'''Crystal structure of P. furiosus Mre11 with manganese and dAMP'''
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[[Category: Tainer, J A.]]
[[Category: Tainer, J A.]]
[[Category: Woo, T T.]]
[[Category: Woo, T T.]]
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[[Category: damp]]
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[[Category: Damp]]
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[[Category: dna double-strand break repair]]
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[[Category: Dna double-strand break repair]]
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[[Category: manganese]]
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[[Category: Manganese]]
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[[Category: mre11]]
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[[Category: Mre11]]
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[[Category: rad50]]
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[[Category: Rad50]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:01:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:13 2008''
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Revision as of 17:01, 2 May 2008

Template:STRUCTURE 1ii7

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. 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 Page seeded by OCA on Fri May 2 20:01:53 2008

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