2J6Y

Structural and Functional Characterisation of partner switching regulating the environmental stress response in Bacillus subtilis

Summary for 2J6Y

• Entry DOI: 10.2210/pdb2j6y/pdb
• Related: 1W53 2J6Z 2J70
• Descriptor: PHOSPHOSERINE PHOSPHATASE RSBU (2 entities in total)
• Functional Keywords: hydrolase, partner switching, protein phosphatase, rsbt, rsbu, stress, bacillus subtilis
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 5
• Total formula weight: 65885.42

Authors

Hardwick, S.W.,Pane-Farre, J.,Delumeau, O.,Marles-Wright, J.,Murray, J.W.,Hecker, M.,Lewis, R.J. (deposition date: 2006-10-05, release date: 2007-02-13, Last modification date: 2023-12-13)

Primary citation

Hardwick, S.W.,Pane-Farre, J.,Delumeau, O.,Marles-Wright, J.,Murray, J.W.,Hecker, M.,Lewis, R.J.
Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.
J. Biol. Chem., 282:11562-11572, 2007

PubMed Abstract: The general stress response of Bacillus subtilis and close relatives provides the cell with protection from a variety of stresses. The upstream component of the environmental stress signal transduction cascade is activated by the RsbT kinase that switches binding partners from a 25 S macromolecular complex, the stressosome, to the RsbU phosphatase. Once the RsbU phosphatase is activated by interacting with RsbT, the alternative sigma factor, sigmaB, directs transcription of the general stress regulon. Previously, we demonstrated that the N-terminal domain of RsbU mediates the binding of RsbT. We now describe residues in N-RsbU that are crucial to this interaction by experimentation both in vitro and in vivo. Furthermore, crystal structures of the N-RsbU mutants provide a molecular explanation for the loss of interaction. Finally, we also characterize mutants in RsbT that affect binding to both RsbU and a simplified, binary model of the stressosome and thus identify overlapping binding surfaces on the RsbT "switch."

PubMed: 17303566
DOI: 10.1074/jbc.M609733200

Experimental method

X-RAY DIFFRACTION (1.85 Å)