2RO5

RDC-refined solution structure of the N-terminal DNA recognition domain of the Bacillus subtilis transition-state regulator SpoVT

Summary for 2RO5

• Entry DOI: 10.2210/pdb2ro5/pdb
• Related: 1Z0R 2FY9 2RO3 2RO4
• NMR Information: BMRB: 11034
• Descriptor: Stage V sporulation protein T (1 entity in total)
• Functional Keywords: transcription, activator, dna-binding, repressor, sporulation, transcription regulation
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 12777.06

Authors

Sullivan, D.M.,Bobay, B.G.,Kojetin, D.J.,Thompson, R.J.,Rance, M.,Strauch, M.A.,Cavanagh, J. (deposition date: 2008-03-08, release date: 2008-11-11, Last modification date: 2024-05-01)

Primary citation

Sullivan, D.M.,Bobay, B.G.,Kojetin, D.J.,Thompson, R.J.,Rance, M.,Strauch, M.A.,Cavanagh, J.
Insights into the nature of DNA binding of AbrB-like transcription factors
Structure, 16:1702-1713, 2008

PubMed Abstract: Understanding the DNA recognition and binding by the AbrB-like family of transcriptional regulators is of significant interest since these proteins enable bacteria to elicit the appropriate response to diverse environmental stimuli. Although these "transition-state regulator" proteins have been well characterized at the genetic level, the general and specific mechanisms of DNA binding remain elusive. We present RDC-refined NMR solution structures and dynamic properties of the DNA-binding domains of three Bacillus subtilis transition-state regulators: AbrB, Abh, and SpoVT. We combined previously investigated DNase I footprinting, DNA methylation, gel-shift assays, and mutagenic and NMR studies to generate a structural model of the complex between AbrBN(55) and its cognate promoter, abrB8. These investigations have enabled us to generate a model for the specific nature of the transition-state regulator-DNA interaction, a structure that has remained elusive thus far.

PubMed: 19000822
DOI: 10.1016/j.str.2008.08.014

Experimental method

SOLUTION NMR