Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome.

Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome.
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DOI:
10.1126/science.1178535
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发表时间:
2009-12-04
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Beckmann R
Beckmann R
中科院分区:
其他
文献类型:
--
作者:
Becker T;Bhushan S;Jarasch A;Armache JP;Funes S;Jossinet F;Gumbart J;Mielke T;Berninghausen O;Schulten K;Westhof E;Gilmore R;Mandon EC;Beckmann R

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The trimeric Sec61/SecY complex is a protein-conducting channel (PCC) for secretory and membrane proteins. Although Sec complexes can form oligomers, it has been suggested that a single copy may serve as an active PCC. We determined sub-nanometer resolution cryo-electron microscopy structures of eukaryotic ribosome-Sec61 complexes. In combination with biochemical data we found that in both idle and active states, the Sec complex is not oligomeric and interacts mainly via two cytoplasmic loops with the universal ribosomal adaptor site. In the active state the ribosomal tunnel and a central pore of the monomeric PCC were occupied by the nascent chain contacting loop 6 of the Sec complex. This provides a structural basis for the activity of a solitary Sec complex in cotranslational protein translocation.
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