2012
The Hexameric Helicase DnaB Adopts a Nonplanar Conformation during Translocation
Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA. The Hexameric Helicase DnaB Adopts a Nonplanar Conformation during Translocation. Cell 2012, 151: 267-277. PMID: 23022319, PMCID: PMC3597440, DOI: 10.1016/j.cell.2012.09.014.Peer-Reviewed Original ResearchConceptsTranslocation mechanismParental duplex DNAReplicative DNA helicaseNucleotides of ssDNAC-terminal domainDNA helicaseDnaB hexamerHelicase DnaBNTP hydrolysisNascent DNAStructural insightsQuaternary structureDNA templateDuplex DNADNA polymeraseDnaBTranslocationSequential hydrolysisSubunitsUnwindingNucleotidesDNASsDNAHelicasesHelicase
2004
Insights 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
1997
Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69
Wang J, Sattar A, Wang C, Karam J, Konigsberg W, Steitz T. Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69. Cell 1997, 89: 1087-1099. PMID: 9215631, DOI: 10.1016/s0092-8674(00)80296-2.Peer-Reviewed Original ResearchBacteriophagesBinding SitesConserved SequenceCrystallographyDNA Polymerase IDNA Polymerase IIDNA, Single-StrandedEscherichia coliExonucleasesGene Expression Regulation, ViralHIVProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryReplication OriginRNA-Directed DNA PolymeraseSequence Homology, Amino Acid
1996
Crystal Structures of an NH2-Terminal Fragment of T4 DNA Polymerase and Its Complexes with Single-Stranded DNA and with Divalent Metal Ions †
Wang J, Yu P, Lin T, Konigsberg W, Steitz T. Crystal Structures of an NH2-Terminal Fragment of T4 DNA Polymerase and Its Complexes with Single-Stranded DNA and with Divalent Metal Ions †. Biochemistry 1996, 35: 8110-8119. PMID: 8679562, DOI: 10.1021/bi960178r.Peer-Reviewed Original ResearchConceptsT4 DNA polymeraseDNA polymeraseExonuclease domainKlenow fragmentExonuclease active siteActive site regionCrystallographic R-factorTranslational regulationMinimal sequence identityMetal ion cofactorsSequence identityActive siteNH2-terminal fragmentNH2-terminalSite regionDivalent metal ion cofactorCarboxylate residuesPolymeraseIon cofactorScissile phosphateEquivalent positionsResidue formsProteinSeparate domainsCrystal structure