6qcm

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'''Unreleased structure'''
 
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The entry 6qcm is ON HOLD until Paper Publication
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==Cryo em structure of the Listeria stressosome==
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<SX load='6qcm' size='340' side='right' viewer='molstar' caption='[[6qcm]], [[Resolution|resolution]] 4.21&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6qcm]] is a 60 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QCM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QCM FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qcm OCA], [http://pdbe.org/6qcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qcm RCSB], [http://www.ebi.ac.uk/pdbsum/6qcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qcm ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 A 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.
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Authors:
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The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation.,Williams AH, Redzej A, Rolhion N, Costa TRD, Rifflet A, Waksman G, Cossart P Nat Commun. 2019 Jul 8;10(1):3005. doi: 10.1038/s41467-019-10782-0. PMID:31285450<ref>PMID:31285450</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6qcm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
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[[Category: Cossart, P]]
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[[Category: Redzej, A]]
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[[Category: Waksman, G]]
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[[Category: Williams, A H]]
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[[Category: Antimicrobial protein]]
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[[Category: Bacteria stress sensor]]
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[[Category: Stress response machine]]
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[[Category: Stressosome complex]]

Current revision

Cryo em structure of the Listeria stressosome

6qcm, resolution 4.21Å

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