2008
Chemical shift mapping of γδ resolvase dimer and activated tetramer: Mechanistic implications for DNA strand exchange
Gehman J, Cocco M, Grindley N. Chemical shift mapping of γδ resolvase dimer and activated tetramer: Mechanistic implications for DNA strand exchange. Biochimica Et Biophysica Acta 2008, 1784: 2086-2092. PMID: 18840551, DOI: 10.1016/j.bbapap.2008.08.023.Peer-Reviewed Original ResearchConceptsDNA strand exchangeStrand exchangeChemical shift mappingWild-type dimerNMR chemical shift assignmentsChemical shift assignmentsDNA recombinaseResolvase dimersX-ray diffraction modelSequence regionsSubunit interfaceTetrameric stateProtomer-protomer interactionsGammadelta resolvaseShift mappingShift assignmentsMechanistic hypothesesStructural variationsResidues
1990
Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction
Hughes R, Hatfull G, Rice P, Steitz T, Grindley N. Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction. Cell 1990, 63: 1331-1338. PMID: 2175679, DOI: 10.1016/0092-8674(90)90428-h.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsHigher-order protein-protein interactionsCooperativity mutantsSite-specific recombinaseGamma delta resolvaseMutant phenotypeResolvase mutantsNucleoprotein complexesCrystallographic tetramersResolvase dimersΓδ resolvaseResolvaseCooperative bindingMutantsDNARecombinationSide chainsRecombinaseProteinInteractionCointegrate intermediatePhenotypeRecombination reactionBindingTetramer