2xxa

From Proteopedia

(Difference between revisions)

Revision as of 10:10, 22 June 2022

The Crystal Structure of the Signal Recognition Particle (SRP) in Complex with its Receptor(SR)

Structural highlights

2xxa is a 6 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1dul, 2xkv, 2j28, 1hq1, 1fts
Activity:	Signal-recognition-particle GTPase, with EC number 3.6.5.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SRP54_ECOLI] 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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] [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.^[8] ^[9] ^[10] ^[11] ^[12] ^[13]

Publication Abstract from PubMed

Cotranslational targeting of membrane and secretory proteins is mediated by the universally conserved signal recognition particle (SRP). Together with its receptor (SR), SRP mediates the guanine triphosphate (GTP)-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. Here, we present the crystal structure of the SRP:SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP:SR guanine triphosphatase (GTPase) complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. Combined with previous findings, these results suggest that the SRP:SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon.

The crystal structure of the signal recognition particle in complex with its receptor.,Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, Doudna JA, Ban N Science. 2011 Feb 18;331(6019):881-6. PMID:21330537^[14]

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

References

↑ Ribes V, Romisch K, Giner A, Dobberstein B, Tollervey D. E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle. Cell. 1990 Nov 2;63(3):591-600. PMID:2171778
↑ Luirink J, High S, Wood H, Giner A, Tollervey D, Dobberstein B. Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex. Nature. 1992 Oct 22;359(6397):741-3. PMID:1279430 doi:http://dx.doi.org/10.1038/359741a0
↑ Phillips GJ, Silhavy TJ. The E. coli ffh gene is necessary for viability and efficient protein export. Nature. 1992 Oct 22;359(6397):744-6. PMID:1331806 doi:http://dx.doi.org/10.1038/359744a0
↑ 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
↑ Froderberg L, Houben EN, Baars L, Luirink J, de Gier JW. Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J Biol Chem. 2004 Jul 23;279(30):31026-32. Epub 2004 May 12. PMID:15140892 doi:10.1074/jbc.M403229200
↑ 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
↑ Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, Doudna JA, Ban N. The crystal structure of the signal recognition particle in complex with its receptor. Science. 2011 Feb 18;331(6019):881-6. PMID:21330537 doi:10.1126/science.1196473

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/2xxa"

@@ Line 3: / Line 3: @@
 <StructureSection load='2xxa' size='340' side='right'caption='[[2xxa]], [[Resolution|resolution]] 3.94&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xxa]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XXA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XXA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xxa]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XXA FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dul|1dul]], [[2xkv|2xkv]], [[2j28|2j28]], [[1hq1|1hq1]], [[1fts|1fts]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dul|1dul]], [[2xkv|2xkv]], [[2j28|2j28]], [[1hq1|1hq1]], [[1fts|1fts]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Signal-recognition-particle_GTPase Signal-recognition-particle GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.4 3.6.5.4] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Signal-recognition-particle_GTPase Signal-recognition-particle GTPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.4 3.6.5.4] </span></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=2xxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxa OCA], [http://pdbe.org/2xxa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xxa RCSB], [http://www.ebi.ac.uk/pdbsum/2xxa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xxa ProSAT]</span></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=2xxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxa OCA], [https://pdbe.org/2xxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xxa RCSB], [https://www.ebi.ac.uk/pdbsum/2xxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xxa ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SRP54_ECOLI SRP54_ECOLI]] 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.<ref>PMID:2171778</ref> <ref>PMID:1279430</ref> <ref>PMID:1331806</ref> <ref>PMID:9305630</ref> <ref>PMID:11735405</ref> <ref>PMID:11741850</ref> <ref>PMID:15140892</ref>  [[http://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>
+[[https://www.uniprot.org/uniprot/SRP54_ECOLI SRP54_ECOLI]] 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.<ref>PMID:2171778</ref> <ref>PMID:1279430</ref> <ref>PMID:1331806</ref> <ref>PMID:9305630</ref> <ref>PMID:11735405</ref> <ref>PMID:11741850</ref> <ref>PMID:15140892</ref>  [[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 ==

2xxa

From Proteopedia

Revision as of 10:10, 22 June 2022

The Crystal Structure of the Signal Recognition Particle (SRP) in Complex with its Receptor(SR)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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