Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5M5H

RIBOSOME-BOUND YIDC INSERTASE

Summary for 5M5H
Entry DOI10.2210/pdb5m5h/pdb
EMDB information4155
DescriptorMembrane protein insertase YidC (1 entity in total)
Functional Keywordsmembrane protein, nanodisc, ribosome ligand, protein transport
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight61872.70
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 citationKedrov, 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: 27974208
DOI: 10.1016/j.celrep.2016.11.059
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.5 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon