3ZTB

The bacterial stressosome: a modular system that has been adapted to control secondary messenger signaling

Summary for 3ZTB

• Entry DOI: 10.2210/pdb3ztb/pdb
• Related: 2VY9 3ZT9 3ZTA 3ZXN
• Descriptor: ANTI-SIGMA-FACTOR ANTAGONIST (STAS) DOMAIN PROTEIN, IODIDE ION (3 entities in total)
• Functional Keywords: signaling, stressosome, signal transduction, phosphorylation, protein-protein interaction, type 2c phosphatases, rsbs
• Biological source: MOORELLA THERMOACETICA
• Total number of polymer chains: 2
• Total formula weight: 27575.69

Authors

Quin, M.B.,Berrisford, J.M.,Newman, J.A.,Basle, A.,Lewis, R.J.,Marles-Wright, J. (deposition date: 2011-07-06, release date: 2012-02-22, Last modification date: 2024-10-16)

Primary citation

Quin, M.B.,Berrisford, J.M.,Newman, J.A.,Basle, A.,Lewis, R.J.,Marles-Wright, J.
The Bacterial Stressosome: A Modular System that Has Been Adapted to Control Secondary Messenger Signaling.
Structure, 20:350-, 2012

PubMed Abstract: The stressosome complex regulates downstream effectors in response to environmental signals. In Bacillus subtilis, it activates the alternative sigma factor σ(B), leading to the upregulation of the general stress regulon. Herein, we characterize a stressosome-regulated biochemical pathway in Moorella thermoacetica. We show that the presumed sensor, MtR, and the scaffold, MtS, form a pseudo-icosahedral structure like that observed in B. subtilis. The N-terminal domain of MtR is structurally homologous to B. subtilis RsbR, despite low sequence identity. The affinity of the switch kinase, MtT, for MtS decreases following MtS phosphorylation and not because of structural reorganization. Dephosphorylation of MtS by the PP2C type phosphatase MtX permits the switch kinase to rebind the stressosome to reset the response. We also show that MtT regulates cyclic di-GMP biosynthesis through inhibition of a GG(D/E)EF-type diguanylate cyclase, demonstrating that secondary messenger levels are regulated by the stressosome.

PubMed: 22325782
DOI: 10.1016/J.STR.2012.01.003

Experimental method

X-RAY DIFFRACTION (2.8 Å)