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[[Image:1ry1.gif|left|200px]]<br /><applet load="1ry1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ry1, resolution 12.&Aring;" />
'''Structure of the signal recognition particle interacting with the elongation-arrested ribosome'''<br />


==Overview==
==Structure of the signal recognition particle interacting with the elongation-arrested ribosome==
Cotranslational translocation of proteins across or into membranes is a vital process in all kingdoms of life. It requires that the translating ribosome be targeted to the membrane by the signal recognition particle (SRP), an evolutionarily conserved ribonucleoprotein particle. SRP recognizes signal sequences of nascent protein chains emerging from the ribosome. Subsequent binding of SRP leads to a pause in peptide elongation and to the ribosome docking to the membrane-bound SRP receptor. Here we present the structure of a targeting complex consisting of mammalian SRP bound to an active 80S ribosome carrying a signal sequence. This structure, solved to 12 A by cryo-electron microscopy, enables us to generate a molecular model of SRP in its functional conformation. The model shows how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation-factor-binding site of the ribosome, explaining its elongation arrest activity.
<SX load='1ry1' size='340' side='right' viewer='molstar' caption='[[1ry1]], [[Resolution|resolution]] 12.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ry1]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RY1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCC:CYTIDINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>CCC</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=1ry1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ry1 OCA], [https://pdbe.org/1ry1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ry1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ry1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ry1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SRP09_HUMAN SRP09_HUMAN] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ry/1ry1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ry1 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1RY1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus], [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] and [http://en.wikipedia.org/wiki/Tursiops_truncatus Tursiops truncatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RY1 OCA].
*[[Avidin 3D structures|Avidin 3D structures]]
 
*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
==Reference==
__TOC__
Structure of the signal recognition particle interacting with the elongation-arrested ribosome., Halic M, Becker T, Pool MR, Spahn CM, Grassucci RA, Frank J, Beckmann R, Nature. 2004 Feb 26;427(6977):808-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14985753 14985753]
</SX>
[[Category: Homo sapiens]]
[[Category: Canis lupus familiaris]]
[[Category: Mus musculus]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Becker T]]
[[Category: Thermus aquaticus]]
[[Category: Beckmann R]]
[[Category: Tursiops truncatus]]
[[Category: Frank J]]
[[Category: Becker, T.]]
[[Category: Grassucci RA]]
[[Category: Beckmann, R.]]
[[Category: Halic M]]
[[Category: Frank, J.]]
[[Category: Pool MR]]
[[Category: Grassucci, R A.]]
[[Category: Spahn CM]]
[[Category: Halic, M.]]
[[Category: Pool, M R.]]
[[Category: Spahn, C M.]]
[[Category: rna binding]]
[[Category: signal recognition particle]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:46 2008''

Latest revision as of 11:26, 14 February 2024

Structure of the signal recognition particle interacting with the elongation-arrested ribosomeStructure of the signal recognition particle interacting with the elongation-arrested ribosome

1ry1, resolution 12.00Å

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