1ii8
From Proteopedia
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|PDB= 1ii8 |SIZE=350|CAPTION= <scene name='initialview01'>1ii8</scene>, resolution 3.02Å | |PDB= 1ii8 |SIZE=350|CAPTION= <scene name='initialview01'>1ii8</scene>, resolution 3.02Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ii7|1II7]], [[1f2t|1F2T]], [[1f2u|1F2U]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ii8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii8 OCA], [http://www.ebi.ac.uk/pdbsum/1ii8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ii8 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Tainer, J A.]] | [[Category: Tainer, J A.]] | ||
[[Category: Woo, T T.]] | [[Category: Woo, T T.]] | ||
| - | [[Category: PO4]] | ||
[[Category: atp]] | [[Category: atp]] | ||
[[Category: dna double-strand break repair]] | [[Category: dna double-strand break repair]] | ||
| Line 34: | Line 36: | ||
[[Category: rad50]] | [[Category: rad50]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:09 2008'' |
Revision as of 18:20, 30 March 2008
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| , resolution 3.02Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1II7, 1F2T, 1F2U
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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