The N-Terminal Domain of the E. coli PriA Helicase Contains Both the DNA- and the Nucleotide-Binding Sites. Energetics of Domain-DNA Interactions and Allosteric Effect of the Nucleotide Cofactors()

Eitemau Tebyg

• The Escherichia coli PriA Helicase–Double-Stranded DNA Complex: Location of the Strong DNA-Binding Subsite on the Helicase Domain of the Protein and the Affinity Control by the Two Nucleotide-Binding Sites of the Enzyme
  gan: Szymanski, Michal R., et al.
  Cyhoeddwyd: (2010)
• The Escherichia coli PriA Helicase Specifically Recognizes Gapped DNA Substrates: EFFECT OF THE TWO NUCLEOTIDE-BINDING SITES OF THE ENZYME ON THE RECOGNITION PROCESS
  gan: Szymanski, Michal R., et al.
  Cyhoeddwyd: (2010)
• Interactions of the Escherichia coli DnaB–DnaC Protein Complex with Nucleotide Cofactors. 1. Allosteric Conformational Transitions of the Complex
  gan: Roychowdhury, Anasuya, et al.
  Cyhoeddwyd: (2009)
• Binding Specificity of E. coli SSB protein for the χ subunit of DNA pol III Holoenzyme and PriA helicase.
  gan: Kozlov, Alexander G., et al.
  Cyhoeddwyd: (2010)
• Escherichia coli DnaB Helicase–DnaC Protein Complex: Allosteric Effects of the Nucleotides on the Nucleic Acid Binding and the Kinetic Mechanism of NTP Hydrolysis. 3
  gan: Roychowdhury, Anasuya, et al.
  Cyhoeddwyd: (2009)