1f2t: Difference between revisions
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[[Image:1f2t.gif|left|200px]] | [[Image:1f2t.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF ATP-FREE RAD50 ABC-ATPASE''' | {{Structure | ||
|PDB= 1f2t |SIZE=350|CAPTION= <scene name='initialview01'>1f2t</scene>, resolution 1.6Å | |||
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'''CRYSTAL STRUCTURE OF ATP-FREE RAD50 ABC-ATPASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F2T is a [ | 1F2T 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=1F2T OCA]. | ||
==Reference== | ==Reference== | ||
Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily., Hopfner KP, Karcher A, Shin DS, Craig L, Arthur LM, Carney JP, Tainer JA, Cell. 2000 Jun 23;101(7):789-800. PMID:[http:// | Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily., Hopfner KP, Karcher A, Shin DS, Craig L, Arthur LM, Carney JP, Tainer JA, Cell. 2000 Jun 23;101(7):789-800. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10892749 10892749] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
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[[Category: dna double-strand break repair]] | [[Category: dna double-strand break repair]] | ||
''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 11:03:35 2008'' | ||
Revision as of 12:03, 20 March 2008
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CRYSTAL STRUCTURE OF ATP-FREE RAD50 ABC-ATPASE
OverviewOverview
To clarify the key role of Rad50 in DNA double-strand break repair (DSBR), we biochemically and structurally characterized ATP-bound and ATP-free Rad50 catalytic domain (Rad50cd) from Pyrococcus furiosus. Rad50cd displays ATPase activity plus ATP-controlled dimerization and DNA binding activities. Rad50cd crystal structures identify probable protein and DNA interfaces and reveal an ABC-ATPase fold, linking Rad50 molecular mechanisms to ABC transporters, including P glycoprotein and cystic fibrosis transmembrane conductance regulator. Binding of ATP gamma-phosphates to conserved signature motifs in two opposing Rad50cd molecules promotes dimerization that likely couples ATP hydrolysis to dimer dissociation and DNA release. These results, validated by mutations, suggest unified molecular mechanisms for ATP-driven cooperativity and allosteric control of ABC-ATPases in DSBR, membrane transport, and chromosome condensation by SMC proteins.
About this StructureAbout this Structure
1F2T is a Protein complex structure of sequences from Pyrococcus furiosus. Full crystallographic information is available from OCA.
ReferenceReference
Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily., Hopfner KP, Karcher A, Shin DS, Craig L, Arthur LM, Carney JP, Tainer JA, Cell. 2000 Jun 23;101(7):789-800. PMID:10892749
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