Signal recognition particle protein: Difference between revisions

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{{STRUCTURE_1e8o|  PDB=1e8o | SIZE=400| SCENE= |right|  CAPTION=Human SRP9 (grey and pink) +SRP14 (green and yellow) complex with 7S RNA, GDP and sulfate [[1e8o]] }}
<StructureSection load='1e8o' size='350' side='right' scene='' caption='Human SRP9 (grey and pink) +SRP14 (green and yellow) complex with 7S RNA, GDP and sulfate [[1e8o]]'>
 
'''Signal recognition particle''' (SRP) is a ribonucleoprotein which targets specific proteins to the endoplasmic reticulum (ER) in eukaryotes and the plasma membrane in prokaryotes.  In eukaryotes SRP binds to the signal sequence of a newly synthesized polypeptide as it emerges from the ribosome.  The binding allows for the coupling of the translation process to the translocation process.  The SRP targets the nascent protein to the ER by docking into the [[Signal recognition particle receptor|SRP receptor]]<ref>PMID:15718142</ref>.  The eukaryotic SRP which has GTPase activity, is composed of SRP9, SRP14<ref>PMID:7542942</ref>, SRP19<ref>PMID:11682607</ref>, SRP54<ref>PMID:9511762</ref>, SRP68, SRP72<ref>PMID:8388879</ref> and 7S RNA.  The prokaryotic SRP is composed of FFH (SRP54-like) and 4.5S RNA.
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'''Signal recognition particle''' (SRP) is a ribonucleoprotein which targets specific proteins to the endoplasmic reticulum (ER) in eukaryotes and the plasma membrane in prokaryotes.  In eukaryotes SRP binds to the signal sequence of a newly synthesized polypeptide as it emerges from the ribosome.  The binding allows for the coupling of the translation process to the translocation process.  The SRP targets the nascent protein to the ER by docking into the [[Signal recognition particle receptor|SRP receptor]].  The eukaryotic SRP which has GTPase activity, is composed of SRP9, SRP14, SRP19, SRP54, SRP68, SRP72 and 7S RNA.  The prokaryotic SRP is composed of FFH (SRP54-like) and 4.5S RNA.
 
==3D structures of SRP==
 
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
[[1914]] – mSRP9/SRP14 – mouse<br />
[[1wgw]] – mSRP54 N terminal – NMR<br />
[[1ls1]], [[2j45]], [[2j46]], [[1ffh]], [[1ng1]], [[3ng1]] - TaSRP54-like NG domain – ''Thermus aquaticus''<br />
[[2ng1]] - TaSRP54-like NG domain (mutant)<br />
[[2ffh]] - TaSRP54-like residues 1-425 (mutant)<br />
[[1kvn]], [[1kvv]] – SRP19 (mutant) – ''Archaeoglobus fulgidus'' – NMR<BR />
[[1qb2]] – hSRP54 <br />
[[2hug]] – AtSRP43 chromo-2 domain + SRP54 M domain – ''Arabidopsis thaliana'' – NMR<BR />
[[3deo]] - AtSRP43 residues 85-267<br />
[[3ui2]] - AtSRP43 residues 84-327 + AtSRP54 RRKR motif<br />
[[3dlu]], [[3dlv]], [[3dm5]] – SRP19 – ''Pyrococcus furiosus''<br />
[[2w9j]] – SRP14 residues 1-91 – fission yeast<br />
[[1j8m]] – AaSPR GTPase domain – ''Acicianus ambivalens''<br />
[[1j8y]] – AaSPR GTPase domain (mutant)<br />
[[1qzx]] – SsSRP54 – ''Sulfolobus solfataricus''<br />
[[4p3f]] – hSRP68 (mutant) – human<br />
 
 
'''SRP complexes with RNA'''
 
[[1e8o]], [[1e8s]] - hSRP9 + hSRP14 + 7S RNA <br />
[[1ry1]] - hSRP9 + hSRP14 + hSRP19 + hSRP54 + 7S RNA<br />
[[1jid]] – hSRP19 + RNA<br />
[[3ktv]] - hSRP19 + RNA S domain<br />
[[3ktw]] - SsSRP19 + RNA S domain <br />
[[1qzw]] – SsSRP + 7S RNA<br />
[[1lng]] – MjSRP19 + RNA – ''Methanocaldococcus jannaschii''<br />
[[1l9a]] - MjSRP19 (mutant) + RNA<br />
[[2v3c]], [[3ndb]] - MjSRP19 + MjSRP54 + 7S RNA<br />
[[1mfq]] – hSRP19 + hSRP54 M domain + 7S RNA S domain<br />
[[2iy3]] – TaSRP54-like + RNA - EM<BR />
[[1dul]], [[1hq1]], [[2pxp]] – EcSRP54-like C terminal + RNA – ''Escherichia coli''<br />
[[3lqx]] - EcSRP54-like + RNA + Co-hexamine<br />
[[2xkv]] - EcSRP54-like NG+M domains + 4.5SRNA – EM<BR />
[[2xxa]] - EcSRP54-like residues 1-433 (mutant) + cell division protein FtsY residues 196-497+ 4.5SRNA<br />
[[3zn8]] - EcSRP54 NG domain + cell division protein FtsY residues 201-495+ 4.5SRNA + dipeptidyl aminopeptidase B<br />
[[2pxb]], [[2pxd]], [[2pxe]], [[2pxf]], [[2pxk]], [[2pxl]], [[2pxq]], [[2pxq]], [[2pxt]], [[2pxu]], [[2pxv]] - EcSRP54-like C terminal + 4.5SRNA domain IV (mutant)<br />
[[2go5]] – dSRP19 + SRP54 + hSRP receptor α subunit + mSRP receptor b subunit + ribosomal proteins L23, L31, L35 + RNA – dog<br />
[[2j28]] – EcSRP54-like + 70S ribosome  – EM<BR />
[[2j37]] - hSRP19 + dSRP54 + ribosomal proteins L23, L31, L35 + RNA – wheat – EM<BR />
 
'''Other SRP complexes'''
 
[[1jpj]], [[1jpn]], [[2c04]] – TaSRP54-like NG domain + GMPPNP<BR />
[[1o87]], [[2c03]] - TaSRP54-like NG domain + GDP<br />
[[1okk]], [[1rj9]], [[2cnw]] - TaSRP54-like NG domain + cell division protein FTSY<br />
[[2j7p]] - TaSRP54-like NG domain + cell division protein FTSY + GMPPNP<BR />
[[3dep]] - AtSRP43 residues 85-267 + polypeptide<br />
[[3kl4]] – SsSRP54 residues 2-432 + polypeptide<br />
[[4c7o]] – EcSRP + FTSY + SRP RNA<br />


==3D structures of signal recognition particle==
[[Signal recognition particle 3D structures]]


== References ==
<references/>
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 13:19, 20 November 2023

Signal recognition particle (SRP) is a ribonucleoprotein which targets specific proteins to the endoplasmic reticulum (ER) in eukaryotes and the plasma membrane in prokaryotes. In eukaryotes SRP binds to the signal sequence of a newly synthesized polypeptide as it emerges from the ribosome. The binding allows for the coupling of the translation process to the translocation process. The SRP targets the nascent protein to the ER by docking into the SRP receptor[1]. The eukaryotic SRP which has GTPase activity, is composed of SRP9, SRP14[2], SRP19[3], SRP54[4], SRP68, SRP72[5] and 7S RNA. The prokaryotic SRP is composed of FFH (SRP54-like) and 4.5S RNA.

3D structures of signal recognition particle

Signal recognition particle 3D structures

References

  1. ↑ Halic M, Beckmann R. The signal recognition particle and its interactions during protein targeting. Curr Opin Struct Biol. 2005 Feb;15(1):116-25. PMID:15718142 doi:http://dx.doi.org/10.1016/j.sbi.2005.01.013
  2. ↑ Bovia F, Fornallaz M, Leffers H, Strub K. The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs. Mol Biol Cell. 1995 Apr;6(4):471-84. PMID:7542942
  3. ↑ Dean KA, von Ahsen O, Gorlich D, Fried HM. Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin. J Cell Sci. 2001 Oct;114(Pt 19):3479-85. PMID:11682607
  4. ↑ Gowda K, Black SD, Moeller I, Sakakibara Y, Liu MC, Zwieb C. Protein SRP54 of human signal recognition particle: cloning, expression, and comparative analysis of functional sites. Gene. 1998 Jan 30;207(2):197-207. PMID:9511762
  5. ↑ Lutcke H, Prehn S, Ashford AJ, Remus M, Frank R, Dobberstein B. Assembly of the 68- and 72-kD proteins of signal recognition particle with 7S RNA. J Cell Biol. 1993 Jun;121(5):977-85. PMID:8388879

Human SRP9 (grey and pink) +SRP14 (green and yellow) complex with 7S RNA, GDP and sulfate 1e8o

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