7o9f: Difference between revisions
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==Bacillus subtilis Ffh in complex with ppGpp== | ==Bacillus subtilis Ffh in complex with ppGpp== | ||
<StructureSection load='7o9f' size='340' side='right'caption='[[7o9f]]' scene=''> | <StructureSection load='7o9f' size='340' side='right'caption='[[7o9f]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O9F FirstGlance]. <br> | <table><tr><td colspan='2'>[[7o9f]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O9F FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7o9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o9f OCA], [https://pdbe.org/7o9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o9f RCSB], [https://www.ebi.ac.uk/pdbsum/7o9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o9f ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G4P:GUANOSINE-5,3-TETRAPHOSPHATE'>G4P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7o9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o9f OCA], [https://pdbe.org/7o9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o9f RCSB], [https://www.ebi.ac.uk/pdbsum/7o9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o9f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/SRP54_BACSU SRP54_BACSU]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components (Probable).<ref>PMID:7511896</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The stringent response enables bacteria to respond to nutrient limitation and other stress conditions through production of the nucleotide-based second messengers ppGpp and pppGpp, collectively known as (p)ppGpp. Here, we report that (p)ppGpp inhibits the signal recognition particle (SRP)-dependent protein targeting pathway, which is essential for membrane protein biogenesis and protein secretion. More specifically, (p)ppGpp binds to the SRP GTPases Ffh and FtsY, and inhibits the formation of the SRP receptor-targeting complex, which is central for the coordinated binding of the translating ribosome to the SecYEG translocon. Cryo-EM analysis of SRP bound to translating ribosomes suggests that (p)ppGpp may induce a distinct conformational stabilization of the NG domain of Ffh and FtsY in Bacillus subtilis but not in E. coli. | |||
Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.,Czech L, Mais CN, Kratzat H, Sarmah P, Giammarinaro P, Freibert SA, Esser HF, Musial J, Berninghausen O, Steinchen W, Beckmann R, Koch HG, Bange G Nat Commun. 2022 Feb 25;13(1):1069. doi: 10.1038/s41467-022-28675-0. PMID:35217658<ref>PMID:35217658</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7o9f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bange G]] | [[Category: Bange, G]] | ||
[[Category: Czech L]] | [[Category: Czech, L]] | ||
[[Category: Mais C | [[Category: Mais, C N]] | ||
[[Category: Alarmone]] | |||
[[Category: Signal recognition particle]] | |||
[[Category: Stress]] | |||
[[Category: Stringent response]] | |||
[[Category: Targeting complex]] | |||
[[Category: Translation]] | |||
Revision as of 10:23, 9 March 2022
Bacillus subtilis Ffh in complex with ppGppBacillus subtilis Ffh in complex with ppGpp
Structural highlights
Function[SRP54_BACSU] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components (Probable).[1] Publication Abstract from PubMedThe stringent response enables bacteria to respond to nutrient limitation and other stress conditions through production of the nucleotide-based second messengers ppGpp and pppGpp, collectively known as (p)ppGpp. Here, we report that (p)ppGpp inhibits the signal recognition particle (SRP)-dependent protein targeting pathway, which is essential for membrane protein biogenesis and protein secretion. More specifically, (p)ppGpp binds to the SRP GTPases Ffh and FtsY, and inhibits the formation of the SRP receptor-targeting complex, which is central for the coordinated binding of the translating ribosome to the SecYEG translocon. Cryo-EM analysis of SRP bound to translating ribosomes suggests that (p)ppGpp may induce a distinct conformational stabilization of the NG domain of Ffh and FtsY in Bacillus subtilis but not in E. coli. Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.,Czech L, Mais CN, Kratzat H, Sarmah P, Giammarinaro P, Freibert SA, Esser HF, Musial J, Berninghausen O, Steinchen W, Beckmann R, Koch HG, Bange G Nat Commun. 2022 Feb 25;13(1):1069. doi: 10.1038/s41467-022-28675-0. PMID:35217658[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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