1ii7
From Proteopedia
(New page: 200px<br /><applet load="1ii7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ii7, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:1ii7.gif|left|200px]]<br /><applet load="1ii7" size=" | + | [[Image:1ii7.gif|left|200px]]<br /><applet load="1ii7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ii7, resolution 2.20Å" /> | caption="1ii7, resolution 2.20Å" /> | ||
'''Crystal structure of P. furiosus Mre11 with manganese and dAMP'''<br /> | '''Crystal structure of P. furiosus Mre11 with manganese and dAMP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To clarify functions of the Mre11/Rad50 (MR) complex in DNA double-strand | + | 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== | ==About this Structure== | ||
| - | 1II7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with PO4, MN, SO4 and DA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1II7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=DA:'>DA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1II7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carney, J | + | [[Category: Carney, J P.]] |
[[Category: Craig, L.]] | [[Category: Craig, L.]] | ||
| - | [[Category: Hopfner, K | + | [[Category: Hopfner, K P.]] |
[[Category: Karcher, A.]] | [[Category: Karcher, A.]] | ||
| - | [[Category: Tainer, J | + | [[Category: Tainer, J A.]] |
| - | [[Category: Woo, T | + | [[Category: Woo, T T.]] |
[[Category: DA]] | [[Category: DA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: rad50]] | [[Category: rad50]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:07 2008'' |
Revision as of 11:12, 21 February 2008
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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 , , and 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
Page seeded by OCA on Thu Feb 21 13:12:07 2008
Categories: Pyrococcus furiosus | Single protein | Carney, J P. | Craig, L. | Hopfner, K P. | Karcher, A. | Tainer, J A. | Woo, T T. | DA | MN | PO4 | SO4 | Damp | Dna double-strand break repair | Manganese | Mre11 | Rad50
