2006
The ϕ29 DNA polymerase:protein‐primer structure suggests a model for the initiation to elongation transition
Kamtekar S, Berman AJ, Wang J, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TA. The ϕ29 DNA polymerase:protein‐primer structure suggests a model for the initiation to elongation transition. The EMBO Journal 2006, 25: 1335-1343. PMID: 16511564, PMCID: PMC1422159, DOI: 10.1038/sj.emboj.7601027.Peer-Reviewed Original ResearchMeSH KeywordsBacillus PhagesBinding SitesCrystallography, X-RayDNA PrimersDNA ReplicationDNA-Directed DNA PolymeraseModels, MolecularMutationPeptide Chain Elongation, TranslationalTranscription, GeneticConceptsTerminal proteinDNA polymeraseDNA synthesisPrime replicationLinear chromosomesElongation transitionϕ29 DNA polymeraseBacteriophage genomesProtein movesBacteriophage phi29Resolution structureDuplex productsElongation phaseBinding cleftThird domainPolymeraseTemplate DNADuplex DNAPrimer strandSerine hydroxylProteinAbsolute requirementDNAActive siteDomain
1994
The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.
Czworkowski J, Wang J, Steitz T, Moore P. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. The EMBO Journal 1994, 13: 3661-3668. PMID: 8070396, PMCID: PMC395276, DOI: 10.1002/j.1460-2075.1994.tb06675.x.Peer-Reviewed Original ResearchAmino Acid SequenceBinding SitesCrystallography, X-RayGTP Phosphohydrolase-Linked Elongation FactorsGuanosine DiphosphateModels, MolecularMolecular Sequence DataPeptide Chain Elongation, TranslationalPeptide Elongation Factor GPeptide Elongation Factor TuPeptide Elongation FactorsThermus thermophilus