DnaA Protein Lys-415 Is Close to the ATP-Binding Site: ATP-Pyridoxal Affinity Labeling

This publication has 25 references indexed in Scilit:

• Functional domains of DnaA proteins
  Biochimie, 1999
• Conformational Transition of DnaA Protein by ATP: Structural Analysis of DnaA Protein, the Initiator ofEscherichia coliChromosome Replication
  Biochemical and Biophysical Research Communications, 1997
• DnaA Protein Is Sensitive to a Soluble Factor and Is Specifically Inactivated for Initiation of in Vitro Replication of the Escherichia coli Minichromosome
  Published by Elsevier ,1995
• Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal: Probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in E. coli methionyl- and valyl-tRNA synthetases
  Biochemistry, 1990
• Identification of α‐subunit Lys²⁰¹ and β‐subunit Lys¹¹⁵ at the ATP‐binding sites inEscherichia coli F₁‐ATPase
  FEBS Letters, 1988
• Adenosine di-, tri- and tetraphosphopyridoxals modify the same lysyl residue at the ATP-binding site in adenylate kinase
  FEBS Letters, 1988
• Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome
  Cell, 1988
• Three-Dimensional Structure of an Oncogene Protein: Catalytic Domain of Human c-H- ras P21
  Science, 1988
• ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
  Cell, 1987
• Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal.
  Biochemistry, 1986