The DNA-binding domain in the Bacillus subtilis transition-state regulator AbrB employs significant motion for promiscuous DNA recognition

This publication has 35 references indexed in Scilit:

• Cooperative Ordering in Homeodomain−DNA Recognition: Solution Structure and Dynamics of the MATa1 Homeodomain
  Biochemistry, 2000
• Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
  Nature, 1999
• Solution NMR Structure and Backbone Dynamics of the Major Cold-Shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dynamics in the Single-Stranded RNA-Binding Site^,
  Biochemistry, 1998
• Long-Range Motional Restrictions in a Multidomain Zinc-Finger Protein from Anisotropic Tumbling
  Science, 1995
• Comparison of the Backbone Dynamics of a Folded and an Unfolded SH3 Domain Existing in Equilibrium in Aqueous Buffer
  Biochemistry, 1995
• 1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG
  Nature Structural & Molecular Biology, 1994
• Modulation of Bacillus subtilis catabolite repression by transition state regulatory protein AbrB
  Journal of Bacteriology, 1994
• Mutant analysis of interaction of the Bacillus subtilis transcription regulator AbrB with the antibiotic biosynthesis gene tycA
  FEBS Letters, 1991
• Interaction of AbrB, a transcriptional regulator from Bacillus subtilis with the promoters of the transition state-activated genes tycA and spoVG
  Molecular Genetics and Genomics, 1991
• Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease
  Biochemistry, 1989