5NCO
Quaternary complex between SRP, SR, and SecYEG bound to the translating ribosome
This is a non-PDB format compatible entry.
Summary for 5NCO
| Entry DOI | 10.2210/pdb5nco/pdb |
| EMDB information | 3617 |
| Descriptor | 4.5S SRP RNA (Ffs), 50S ribosomal protein L9, 50S ribosomal protein L10, ... (44 entities in total) |
| Functional Keywords | ribosome, srp, sec translocon, srp receptor, quaternary complex |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P0AGA2 P0AG96 P0AG99 Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : P10121 |
| Total number of polymer chains | 40 |
| Total formula weight | 1541118.44 |
| Authors | Jomaa, A.,Hwang Fu, Y.,Boerhinger, D.,Leibundgut, M.,Shan, S.O.,Ban, N. (deposition date: 2017-03-06, release date: 2016-01-27, Last modification date: 2025-04-09) |
| Primary citation | Jomaa, A.,Fu, Y.H.,Boehringer, D.,Leibundgut, M.,Shan, S.O.,Ban, N. Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome. Nat Commun, 8:15470-15470, 2017 Cited by PubMed Abstract: During co-translational protein targeting, the signal recognition particle (SRP) binds to the translating ribosome displaying the signal sequence to deliver it to the SRP receptor (SR) on the membrane, where the signal peptide is transferred to the translocon. Using electron cryo-microscopy, we have determined the structure of a quaternary complex of the translating Escherichia coli ribosome, the SRP-SR in the 'activated' state and the translocon. Our structure, supported by biochemical experiments, reveals that the SRP RNA adopts a kinked and untwisted conformation to allow repositioning of the 'activated' SRP-SR complex on the ribosome. In addition, we observe the translocon positioned through interactions with the SR in the vicinity of the ribosome exit tunnel where the signal sequence is extending beyond its hydrophobic binding groove of the SRP M domain towards the translocon. Our study provides new insights into the mechanism of signal sequence transfer from the SRP to the translocon. PubMed: 28524878DOI: 10.1038/ncomms15470 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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