+Search query
-Structure paper
Title | Molecular insights into intra-complex signal transmission during stressosome activation. |
---|---|
Journal, issue, pages | Commun Biol, Vol. 5, Issue 1, Page 621, Year 2022 |
Publish date | Jun 27, 2022 |
Authors | Algirdas Miksys / Lifei Fu / M Gregor Madej / Duarte N Guerreiro / Susann Kaltwasser / Maria Conway / Sema Ejder / Astrid Bruckmann / Jon Marles-Wright / Richard J Lewis / Conor O'Byrne / Jan Pané-Farré / Christine Ziegler / |
PubMed Abstract | The stressosome is a pseudo-icosahedral megadalton bacterial stress-sensing protein complex consisting of several copies of two STAS-domain proteins, RsbR and RsbS, and the kinase RsbT. Upon ...The stressosome is a pseudo-icosahedral megadalton bacterial stress-sensing protein complex consisting of several copies of two STAS-domain proteins, RsbR and RsbS, and the kinase RsbT. Upon perception of environmental stress multiple copies of RsbT are released from the surface of the stressosome. Free RsbT activates downstream proteins to elicit a global cellular response, such as the activation of the general stress response in Gram-positive bacteria. The molecular events triggering RsbT release from the stressosome surface remain poorly understood. Here we present the map of Listeria innocua RsbR1/RsbS complex at resolutions of 3.45 Å for the STAS domain core in icosahedral symmetry and of 3.87 Å for the STAS domain and N-terminal sensors in D2 symmetry, respectively. The structure reveals a conformational change in the STAS domain linked to phosphorylation in RsbR. Docking studies indicate that allosteric RsbT binding to the conformationally flexible N-terminal sensor domain of RsbR affects the affinity of RsbS towards RsbT. Our results bring to focus the molecular events within the stressosome complex and further our understanding of this ubiquitous signaling hub. |
External links | Commun Biol / PubMed:35760945 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.86 Å |
Structure data | EMDB-11971, PDB-7b0u: |
Source |
|
Keywords | SIGNALING PROTEIN / Stressosome / stress sensing / general stress response / phosphorylation cascade |