1f2u
CRYSTAL STRUCTURE OF RAD50 ABC-ATPASE
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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
1F2U is a Protein complex structure of sequences from Pyrococcus furiosus with MG and ATP as ligands. 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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