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2WWA

Cryo-EM structure of idle yeast Ssh1 complex bound to the yeast 80S ribosome

Summary for 2WWA
Entry DOI10.2210/pdb2wwa/pdb
Related1K5Y 1S1I 2WWA 2WWB
EMDB information1651 1652 1667 1668 1669
DescriptorSEC SIXTY-ONE PROTEIN HOMOLOG, 60S RIBOSOMAL PROTEIN L19, 60S RIBOSOMAL PROTEIN L25, ... (15 entities in total)
Functional Keywordsribosomal protein, ribonucleoprotein, transmembrane, phosphoprotein, signal sequence, membrane, ribosome, transport, rna-binding, rrna-binding, translocation, protein conducting channel, protein exit tunnel, endoplasmic reticulum, cotranslational protein translocation, isopeptide bond, protein transport
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
More
Total number of polymer chains15
Total formula weight261775.87
Authors
Primary citationBecker, T.,Bhushan, S.,Jarasch, A.,Armache, J.P.,Funes, S.,Jossinet, F.,Gumbart, J.,Mielke, T.,Berninghausen, O.,Schulten, K.,Westhof, E.,Gilmore, R.,Mandon, E.,Beckmann, R.
Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome.
Science, 326:1369-, 2009
Cited by
PubMed Abstract: 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 subnanometer-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.
PubMed: 19933108
DOI: 10.1126/SCIENCE.1178535
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8.9 Å)
Structure validation

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数据于2024-11-06公开中

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