1ii8
From Proteopedia
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| - | [[Image:1ii8.gif|left|200px]] | + | [[Image:1ii8.gif|left|200px]] |
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| - | '''Crystal structure of the P. furiosus Rad50 ATPase domain''' | + | {{Structure |
| + | |PDB= 1ii8 |SIZE=350|CAPTION= <scene name='initialview01'>1ii8</scene>, resolution 3.02Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the P. furiosus Rad50 ATPase domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1II8 is a [ | + | 1II8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1II8 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11371344 11371344] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
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[[Category: rad50]] | [[Category: rad50]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:42 2008'' |
Revision as of 09:50, 20 March 2008
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| , resolution 3.02Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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