1l8d: Difference between revisions
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'''Rad50 coiled-coil Zn hook''' | {{Structure | ||
|PDB= 1l8d |SIZE=350|CAPTION= <scene name='initialview01'>1l8d</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Rad50 coiled-coil Zn hook''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L8D is a [ | 1L8D is a [[Single protein]] structure of sequence 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=1L8D OCA]. | ||
==Reference== | ==Reference== | ||
The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair., Hopfner KP, Craig L, Moncalian G, Zinkel RA, Usui T, Owen BA, Karcher A, Henderson B, Bodmer JL, McMurray CT, Carney JP, Petrini JH, Tainer JA, Nature. 2002 Aug 1;418(6897):562-6. PMID:[http:// | The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair., Hopfner KP, Craig L, Moncalian G, Zinkel RA, Usui T, Owen BA, Karcher A, Henderson B, Bodmer JL, McMurray CT, Carney JP, Petrini JH, Tainer JA, Nature. 2002 Aug 1;418(6897):562-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12152085 12152085] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''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 12:27:50 2008'' | ||
Revision as of 13:27, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Rad50 coiled-coil Zn hook
OverviewOverview
The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. These functions all imply that the linked binding of two DNA substrates occurs, although the molecular basis for this process remains unknown. Here we present a 2.2 A crystal structure of the Rad50 coiled-coil region that reveals an unexpected dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn(2+) ion. Biochemical, X-ray and electron microscopy data indicate that these hooks can join oppositely protruding Rad50 coiled-coil domains to form a flexible bridge of up to 1,200 A. This suggests a function for the long insertion in the Rad50 ABC-ATPase domain. The Rad50 hook is functional, because mutations in this motif confer radiation sensitivity in yeast and disrupt binding at the distant Mre11 nuclease interface. These data support an architectural role for the Rad50 coiled coils in forming metal-mediated bridging complexes between two DNA-binding heads. The resulting assemblies have appropriate lengths and conformational properties to link sister chromatids in homologous recombination and DNA ends in non-homologous end-joining.
About this StructureAbout this Structure
1L8D is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
ReferenceReference
The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair., Hopfner KP, Craig L, Moncalian G, Zinkel RA, Usui T, Owen BA, Karcher A, Henderson B, Bodmer JL, McMurray CT, Carney JP, Petrini JH, Tainer JA, Nature. 2002 Aug 1;418(6897):562-6. PMID:12152085
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