5M5H
RIBOSOME-BOUND YIDC INSERTASE
Summary for 5M5H
Entry DOI | 10.2210/pdb5m5h/pdb |
EMDB information | 4155 |
Descriptor | Membrane protein insertase YidC (1 entity in total) |
Functional Keywords | membrane protein, nanodisc, ribosome ligand, protein transport |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 61872.70 |
Authors | Kedrov, A.,Wickles, S.,Crevenna, A.H.,van der Sluis, E.,Buschauer, R.,Berninghausen, O.,Lamb, D.C.,Beckmann, R. (deposition date: 2016-10-21, release date: 2016-12-14, Last modification date: 2024-05-08) |
Primary citation | Kedrov, A.,Wickles, S.,Crevenna, A.H.,van der Sluis, E.O.,Buschauer, R.,Berninghausen, O.,Lamb, D.C.,Beckmann, R. Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis. Cell Rep, 17:2943-2954, 2016 Cited by PubMed Abstract: Members of the YidC/Oxa1/Alb3 family universally facilitate membrane protein biogenesis, via mechanisms that have thus far remained unclear. Here, we investigated two crucial functional aspects: the interaction of YidC with ribosome:nascent chain complexes (RNCs) and the structural dynamics of RNC-bound YidC in nanodiscs. We observed that a fully exposed nascent transmembrane domain (TMD) is required for high-affinity YidC:RNC interactions, while weaker binding may already occur at earlier stages of translation. YidC efficiently catalyzed the membrane insertion of nascent TMDs in both fluid and gel phase membranes. Cryo-electron microscopy and fluorescence analysis revealed a conformational change in YidC upon nascent chain insertion: the essential TMDs 2 and 3 of YidC were tilted, while the amphipathic helix EH1 relocated into the hydrophobic core of the membrane. We suggest that EH1 serves as a mechanical lever, facilitating a coordinated movement of YidC TMDs to trigger the release of nascent chains into the membrane. PubMed: 27974208DOI: 10.1016/j.celrep.2016.11.059 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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