2go5: Difference between revisions
New page: left|200px<br /> <applet load="2go5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2go5, resolution 7.4Å" /> '''Structure of signal ... |
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[[Image:2go5.gif|left|200px]]<br /> | [[Image:2go5.gif|left|200px]]<br /><applet load="2go5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2go5, resolution 7.4Å" /> | caption="2go5, resolution 7.4Å" /> | ||
'''Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex'''<br /> | '''Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex'''<br /> | ||
==Overview== | ==Overview== | ||
Signal sequences of secretory and membrane proteins are recognized by the | Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo-electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain-mediated elongation arrest persisted. | ||
==About this Structure== | ==About this Structure== | ||
2GO5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Conyza_sp. Conyza sp.], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Triticum_sp. Triticum sp.]. Full crystallographic information is available from [http:// | 2GO5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Conyza_sp. Conyza sp.], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Triticum_sp. Triticum sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GO5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Halic, M.]] | [[Category: Halic, M.]] | ||
[[Category: Mielke, T.]] | [[Category: Mielke, T.]] | ||
[[Category: Pool, M | [[Category: Pool, M R.]] | ||
[[Category: Schlenker, O.]] | [[Category: Schlenker, O.]] | ||
[[Category: Sinning, I.]] | [[Category: Sinning, I.]] | ||
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[[Category: srp]] | [[Category: srp]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:39 2008'' | ||
Revision as of 18:33, 21 February 2008
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Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex
OverviewOverview
Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo-electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain-mediated elongation arrest persisted.
About this StructureAbout this Structure
2GO5 is a Protein complex structure of sequences from Conyza sp., Homo sapiens, Mus musculus and Triticum sp.. Full crystallographic information is available from OCA.
ReferenceReference
Signal recognition particle receptor exposes the ribosomal translocon binding site., Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R, Science. 2006 May 5;312(5774):745-7. PMID:16675701
Page seeded by OCA on Thu Feb 21 17:33:39 2008