2VY9
Molecular architecture of the stressosome, a signal integration and transduction hub
Summary for 2VY9
Entry DOI | 10.2210/pdb2vy9/pdb |
Descriptor | ANTI-SIGMA-FACTOR ANTAGONIST (2 entities in total) |
Functional Keywords | moorella thermoacetica, gene regulation, rsbs, stressosome, stas domain, bacillus subtilis |
Biological source | MOORELLA THERMOACETICA |
Total number of polymer chains | 2 |
Total formula weight | 27537.09 |
Authors | Marles-Wright, J.,Grant, T.,Delumeau, O.,van Duinen, G.,Firbank, S.J.,Lewis, P.J.,Murray, J.W.,Newman, J.A.,Quin, M.B.,Race, P.R.,Rohou, A.,Tichelaar, W.,van Heel, M.,Lewis, R.J. (deposition date: 2008-07-21, release date: 2008-10-14, Last modification date: 2024-10-16) |
Primary citation | Marles-Wright, J.,Grant, T.,Delumeau, O.,Van Duinen, G.,Firbank, S.J.,Lewis, P.J.,Murray, J.W.,Newman, J.A.,Quin, M.B.,Race, P.R.,Rohou, A.,Tichelaar, W.,Van Heel, M.,Lewis, R.J. Molecular Architecture of the "Stressosome," a Signal Integration and Transduction Hub Science, 322:92-, 2008 Cited by PubMed Abstract: A commonly used strategy by microorganisms to survive multiple stresses involves a signal transduction cascade that increases the expression of stress-responsive genes. Stress signals can be integrated by a multiprotein signaling hub that responds to various signals to effect a single outcome. We obtained a medium-resolution cryo-electron microscopy reconstruction of the 1.8-megadalton "stressosome" from Bacillus subtilis. Fitting known crystal structures of components into this reconstruction gave a pseudoatomic structure, which had a virus capsid-like core with sensory extensions. We suggest that the different sensory extensions respond to different signals, whereas the conserved domains in the core integrate the varied signals. The architecture of the stressosome provides the potential for cooperativity, suggesting that the response could be tuned dependent on the magnitude of chemophysical insult. PubMed: 18832644DOI: 10.1126/SCIENCE.1159572 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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