2j37: Difference between revisions
New page: left|200px<br /> <applet load="2j37" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j37, resolution 8.0Å" /> '''MODEL OF MAMMALIAN S... |
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[[Image:2j37.gif|left|200px]]<br /> | [[Image:2j37.gif|left|200px]]<br /><applet load="2j37" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2j37, resolution 8.0Å" /> | caption="2j37, resolution 8.0Å" /> | ||
'''MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS'''<br /> | '''MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS'''<br /> | ||
==Overview== | ==Overview== | ||
Membrane and secretory proteins can be co-translationally inserted into or | Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting. | ||
==About this Structure== | ==About this Structure== | ||
2J37 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris], [http://en.wikipedia.org/wiki/Conyza_sp. Conyza sp.], [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http:// | 2J37 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris], [http://en.wikipedia.org/wiki/Conyza_sp. Conyza sp.], [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J37 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: Sinning, I.]] | [[Category: Sinning, I.]] | ||
[[Category: Wild, K.]] | [[Category: Wild, K.]] | ||
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[[Category: translation/rna]] | [[Category: translation/rna]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:42 2008'' | ||
Revision as of 18:58, 21 February 2008
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MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS
OverviewOverview
Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting.
About this StructureAbout this Structure
2J37 is a Protein complex structure of sequences from Canis lupus familiaris, Conyza sp., Haloarcula marismortui, Homo sapiens and Triticum aestivum. Full crystallographic information is available from OCA.
ReferenceReference
Following the signal sequence from ribosomal tunnel exit to signal recognition particle., Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R, Nature. 2006 Nov 23;444(7118):507-11. Epub 2006 Oct 29. PMID:17086193
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