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-Structure paper
タイトル | The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 3005, Year 2019 |
掲載日 | 2019年7月8日 |
著者 | Allison H Williams / Adam Redzej / Nathalie Rolhion / Tiago R D Costa / Aline Rifflet / Gabriel Waksman / Pascale Cossart / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:31285450 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.37 - 4.21 Å |
構造データ | EMDB-4510: |
由来 |
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キーワード | ANTIMICROBIAL PROTEIN (抗微生物ペプチド) / Stressosome complex / stress response machine / Bacteria stress sensor |