1991
The 3′‐5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction.
Derbyshire V, Grindley N, Joyce C. The 3′‐5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. The EMBO Journal 1991, 10: 17-24. PMID: 1989882, PMCID: PMC452606, DOI: 10.1002/j.1460-2075.1991.tb07916.x.Peer-Reviewed Original ResearchConceptsActive siteMetal ionsEnzyme-bound metal ionSide chainsExonuclease reactionDivalent metal ionsAmino acid side chainsCarboxylate side chainAcid side chainsHydroxide ionMetal ligandsNucleophilic attackIonsTerminal phosphodiester bondPhosphodiester bondReactionExonuclease active siteActivity resultsKlenow fragmentDuplex DNA substratesCatalysisChainCarboxylateTerminal baseSubstrate
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 reactionBindingTetramerThe crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution
Sanderson M, Freemont P, Rice P, Goldman A, Hatfull G, Grindley N, Steitz T. The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution. Cell 1990, 63: 1323-1329. PMID: 2175678, DOI: 10.1016/0092-8674(90)90427-g.Peer-Reviewed Original Research