2iy3

From Proteopedia

(Difference between revisions)

Current revision

Structure of the E. Coli Signal Regognition Particle

2iy3, resolution 16.00Å

Structural highlights

2iy3 is a 3 chain structure with sequence from Escherichia coli, Saccharolobus solfataricus, Thermus aquaticus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 16Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SRP54_THEAQ 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 (By similarity).[HAMAP-Rule:MF_00306]SRP54_SACS2 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.[HAMAP-Rule:MF_00306]

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The prokaryotic signal recognition particle (SRP) targets membrane proteins into the inner membrane. It binds translating ribosomes and screens the emerging nascent chain for a hydrophobic signal sequence, such as the transmembrane helix of inner membrane proteins. If such a sequence emerges, the SRP binds tightly, allowing the SRP receptor to lock on. This assembly delivers the ribosome-nascent chain complex to the protein translocation machinery in the membrane. Using cryo-electron microscopy and single-particle reconstruction, we obtained a 16 A structure of the Escherichia coli SRP in complex with a translating E. coli ribosome containing a nascent chain with a transmembrane helix anchor. We also obtained structural information on the SRP bound to an empty E. coli ribosome. The latter might share characteristics with a scanning SRP complex, whereas the former represents the next step: the targeting complex ready for receptor binding. High-resolution structures of the bacterial ribosome and of the bacterial SRP components are available, and their fitting explains our electron microscopic density. The structures reveal the regions that are involved in complex formation, provide insight into the conformation of the SRP on the ribosome and indicate the conformational changes that accompany high-affinity SRP binding to ribosome nascent chain complexes upon recognition of the signal sequence.

Structure of the E. coli signal recognition particle bound to a translating ribosome.,Schaffitzel C, Oswald M, Berger I, Ishikawa T, Abrahams JP, Koerten HK, Koning RI, Ban N Nature. 2006 Nov 23;444(7118):503-6. Epub 2006 Oct 29. PMID:17086205^[1]

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

References

↑ Schaffitzel C, Oswald M, Berger I, Ishikawa T, Abrahams JP, Koerten HK, Koning RI, Ban N. Structure of the E. coli signal recognition particle bound to a translating ribosome. Nature. 2006 Nov 23;444(7118):503-6. Epub 2006 Oct 29. PMID:17086205 doi:10.1038/nature05182

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iy3"

@@ Line 3: / Line 3: @@
 <SX load='2iy3' size='340' side='right' viewer='molstar' caption='[[2iy3]], [[Resolution|resolution]] 16.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iy3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iy3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus], [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY3 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">srp54, SULA_1982, SULB_1983, SULC_1981 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 ATCC 25104])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 16&#8491;</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=2iy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy3 OCA], [https://pdbe.org/2iy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iy3 RCSB], [https://www.ebi.ac.uk/pdbsum/2iy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SRP54_THEAQ SRP54_THEAQ]] 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 (By similarity).[HAMAP-Rule:MF_00306]
+[https://www.uniprot.org/uniprot/SRP54_THEAQ SRP54_THEAQ] 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 (By similarity).[HAMAP-Rule:MF_00306][https://www.uniprot.org/uniprot/SRP54_SACS2 SRP54_SACS2] 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.[HAMAP-Rule:MF_00306]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Signal recognition particle protein|Signal recognition particle protein]]
+*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Atcc 25104]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Abrahams, J P]]
+[[Category: Saccharolobus solfataricus]]
-[[Category: Ban, N]]
+[[Category: Synthetic construct]]
-[[Category: Berger, I]]
+[[Category: Thermus aquaticus]]
-[[Category: Ishikawa, T]]
+[[Category: Abrahams JP]]
-[[Category: Koerten, H K]]
+[[Category: Ban N]]
-[[Category: Koning, R I]]
+[[Category: Berger I]]
-[[Category: Oswald, M]]
+[[Category: Ishikawa T]]
-[[Category: Schaffitzel, C]]
+[[Category: Koerten HK]]
-[[Category: Rna-binding]]
+[[Category: Koning RI]]
-[[Category: Rna-binding protein complex]]
+[[Category: Oswald M]]
-[[Category: Signal recognition particle]]
+[[Category: Schaffitzel C]]

2iy3

From Proteopedia

Current revision

Structure of the E. Coli Signal Regognition Particle

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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