title: Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex.
abstract: The Bacillus subtilis Spx protein is a global transcription factor that interacts with the C-terminal domain of the RNA polymerase alpha subunit (alphaCTD) and regulates transcription of genes involved in thiol-oxidative stress, sporulation, competence, and organosulfur metabolism. Here we determined the X-ray crystal structure of the Spx/alphaCTD complex from an entirely new crystal form than previously reported [Newberry, K.J., Nakano, S., Zuber, P., Brennan, R.G., 2005. Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc. Natl. Acad. Sci. USA 102, 15839-15844]. Comparison of the previously reported sulfate-bound complex and our sulfate-free complex reveals subtle conformational changes that may be important for the role of Spx in regulating organosulfur metabolism.
authors: The Rockefeller University, New York, NY 10065, USA.
authors: Valerie
authors: V
authors: Lamour
authors: Lars F
authors: LF
authors: Westblade
authors: Elizabeth A
authors: EA
authors: Campbell
authors: Seth A
authors: SA
authors: Darst
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D018360:Crystallography, X-Ray / Q000379:methods*; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D012321:DNA-Directed RNA Polymerases; C113275:RNA polymerase alpha subunit