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9RBF

Structure of a stalled E. coli 70S RNC-NuoK-86 in complex with the membrane protein insertase SecYEG-YidC

This is a non-PDB format compatible entry.
Summary for 9RBF
Entry DOI10.2210/pdb9rbf/pdb
EMDB information53892 53894
DescriptorLarge ribosomal subunit protein bL33, Membrane protein insertase YidC, 16S rRNA, ... (65 entities in total)
Functional Keywords70s ribosome, secyeg translocon, yidc, nuok, protein transport
Biological sourceEscherichia coli
More
Total number of polymer chains61
Total formula weight2349741.37
Authors
Rosales-Hernandez, C.,Busch, M.,Kamel, M.,Beckmann, R.,Kedrov, A. (deposition date: 2025-05-22, release date: 2026-06-03, Last modification date: 2026-07-08)
Primary citationBusch, M.,Rosales-Hernandez, C.,Kamel, M.,Schaumkessel, Y.,van der Sluis, E.O.,Berninghausen, O.,Becker, T.,Beckmann, R.,Kedrov, A.
Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.
Embo J., 2026
Cited by
PubMed Abstract: The Sec translocon and the YidC/Oxa1-type insertases universally mediate biogenesis of α-helical membrane proteins, but the molecular basis of their cooperation has remained disputed. Recent discovery of multi-subunit insertases assembled at the back of the translocon in fungi and higher eukaryotes has raised questions about the architecture and mechanism of the putative bacterial ortholog SecYEG-YidC. Here, we combine cryogenic electron microscopy with cell-free protein synthesis to visualize biogenesis of the SecYEG/YidC-dependent multipass membrane protein NuoK. The nascent chain of NuoK does not enter the lateral gate of SecYEG but instead crosses the translocon towards its back side, where YidC is recruited in the nascent substrate-dependent manner. The SecY-YidC interface promotes folding of the transmembrane helices before insertion, consistent with thermodynamic principles of membrane protein folding. YidC forms extensive contacts with the nascent chain, suggesting its key role in the insertion event. These findings provide mechanistic insight into membrane protein insertases, support evolutionary conservation of a gate-independent insertion route, and expand current models of membrane protein biogenesis.
PubMed: 42362696
DOI: 10.1038/s44318-026-00837-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.44 Å)
Structure validation

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