Summary for 6QCM
| Entry DOI | 10.2210/pdb6qcm/pdb |
| EMDB information | 4508 |
| Descriptor | RsbR protein, RsbS protein, RsbR protein,RsbR protein, ... (5 entities in total) |
| Functional Keywords | stressosome complex, stress response machine, bacteria stress sensor, antimicrobial protein |
| Biological source | Listeria monocytogenes EGD-e More |
| Total number of polymer chains | 60 |
| Total formula weight | 812972.93 |
| Authors | Williams, A.H.,Redzej, A.,Waksman, G.,Cossart, P. (deposition date: 2018-12-28, release date: 2019-08-21, Last modification date: 2024-11-13) |
| Primary citation | Williams, A.H.,Redzej, A.,Rolhion, N.,Costa, T.R.D.,Rifflet, A.,Waksman, G.,Cossart, P. The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation. Nat Commun, 10:3005-3005, 2019 Cited by PubMed Abstract: How the stressosome, the epicenter of the stress response in bacteria, transmits stress signals from the environment has remained elusive. The stressosome consists of multiple copies of three proteins RsbR, RsbS and RsbT, a kinase that is important for its activation. Using cryo-electron microscopy, we determined the atomic organization of the Listeria monocytogenes stressosome at 3.38 Å resolution. RsbR and RsbS are organized in a 60-protomers truncated icosahedron. A key phosphorylation site on RsbR (T209) is partially hidden by an RsbR flexible loop, whose "open" or "closed" position could modulate stressosome activity. Interaction between three glutamic acids in the N-terminal domain of RsbR and the membrane-bound mini-protein Prli42 is essential for Listeria survival to stress. Together, our data provide the atomic model of the stressosome core and highlight a loop important for stressosome activation, paving the way towards elucidating the mechanism of signal transduction by the stressosome in bacteria. PubMed: 31285450DOI: 10.1038/s41467-019-10782-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.21 Å) |
Structure validation
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