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 ResearchConceptsTerminal proteinDNA polymeraseDNA synthesisPrime replicationLinear chromosomesElongation transitionϕ29 DNA polymeraseBacteriophage genomesProtein movesBacteriophage phi29Resolution structureDuplex productsElongation phaseBinding cleftThird domainPolymeraseTemplate DNADuplex DNAPrimer strandSerine hydroxylProteinAbsolute requirementDNAActive siteDomain
2004
Correction of X‐ray intensities from single crystals containing lattice‐translocation defects
Wang J, Kamtekar S, Berman AJ, Steitz TA. Correction of X‐ray intensities from single crystals containing lattice‐translocation defects. Acta Crystallographica Section D, Structural Biology 2004, 61: 67-74. PMID: 15608377, DOI: 10.1107/s0907444904026721.Peer-Reviewed Original ResearchInsights into Strand Displacement and Processivity from the Crystal Structure of the Protein-Primed DNA Polymerase of Bacteriophage φ29
Kamtekar S, Berman AJ, Wang J, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TA. Insights into Strand Displacement and Processivity from the Crystal Structure of the Protein-Primed DNA Polymerase of Bacteriophage φ29. Molecular Cell 2004, 16: 609-618. PMID: 15546620, DOI: 10.1016/j.molcel.2004.10.019.Peer-Reviewed Original ResearchConceptsDNA polymerasePhi29 DNA polymeraseT7 RNA polymeraseB-family polymerasesSpecific serinePriming proteinPolymerase active sitePhage phi29RNA polymerasePhage genomeSpecificity loopNontemplate strandStrand displacement activityFirst nucleotideHomology modelingSequence insertionHigh processivityProtein primerB familyPolymeraseDuplex DNATemplate DNAProcessivityProteinDNA