7o9h

From Proteopedia

(Difference between revisions)

Revision as of 10:05, 27 September 2023

Escherichia coli FtsY in complex with pppGpp

Structural highlights

7o9h is a 2 chain structure with sequence from Escherichia coli DH5alpha. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FTSY_ECOLI Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC 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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Luirink J, ten Hagen-Jongman CM, van der Weijden CC, Oudega B, High S, Dobberstein B, Kusters R. An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY. EMBO J. 1994 May 15;13(10):2289-96. PMID:8194520
↑ Powers T, Walter P. Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J. 1997 Aug 15;16(16):4880-6. PMID:9305630 doi:10.1093/emboj/16.16.4880
↑ Peluso P, Shan SO, Nock S, Herschlag D, Walter P. Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry. 2001 Dec 18;40(50):15224-33. PMID:11735405
↑ Tian H, Beckwith J. Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway. J Bacteriol. 2002 Jan;184(1):111-8. PMID:11741850
↑ Buskiewicz I, Deuerling E, Gu SQ, Jockel J, Rodnina MV, Bukau B, Wintermeyer W. Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor. Proc Natl Acad Sci U S A. 2004 May 25;101(21):7902-6. Epub 2004 May 17. PMID:15148364 doi:http://dx.doi.org/10.1073/pnas.0402231101
↑ Shan SO, Chandrasekar S, Walter P. Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation. J Cell Biol. 2007 Aug 13;178(4):611-20. Epub 2007 Aug 6. PMID:17682051 doi:http://dx.doi.org/10.1083/jcb.200702018
↑ 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. Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp. Nat Commun. 2022 Feb 25;13(1):1069. doi: 10.1038/s41467-022-28675-0. PMID:35217658 doi:http://dx.doi.org/10.1038/s41467-022-28675-0

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7o9h"

Categories: Large Structures | Bange G | Czech L | Mais C-N

@@ Line 3: / Line 3: @@
 <StructureSection load='7o9h' size='340' side='right'caption='[[7o9h]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7o9h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O9H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7o9h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH5alpha Escherichia coli DH5alpha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O9H FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1Z:guanosine+3-diphosphate+5-triphosphate'>C1Z</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1Z:guanosine+3-diphosphate+5-triphosphate'>C1Z</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=7o9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o9h OCA], [https://pdbe.org/7o9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o9h RCSB], [https://www.ebi.ac.uk/pdbsum/7o9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o9h ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/FTSY_ECOLI FTSY_ECOLI] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC 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.<ref>PMID:8194520</ref> <ref>PMID:9305630</ref> <ref>PMID:11735405</ref> <ref>PMID:11741850</ref> <ref>PMID:15148364</ref> <ref>PMID:17682051</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 19: @@
 </div>
 <div class="pdbe-citations 7o9h" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Signal recognition particle receptor|Signal recognition particle receptor]]
 == References ==
 <references/>
@@ Line 21: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Bange, G]]
+[[Category: Bange G]]
-[[Category: Czech, L]]
+[[Category: Czech L]]
-[[Category: Mais, C N]]
+[[Category: Mais C-N]]
-[[Category: Alarmone]]
-[[Category: Signal recognition particle]]
-[[Category: Stress]]
-[[Category: Stringent response]]
-[[Category: Targeting complex]]
-[[Category: Translation]]

7o9h

From Proteopedia

Revision as of 10:05, 27 September 2023

Escherichia coli FtsY in complex with pppGpp

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox