5A7U: Single-particle cryo-EM of co-translational folded adr1 domain inside the E. coli ribosome exit tunnel

At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of cotranslational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
PDB ID: 5A7UDownload
MMDB ID: 132665
PDB Deposition Date: 2015/7/10
Updated in MMDB: 2017/09
Experimental Method:
electron microscopy
Resolution: 4.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5A7U: monomeric; determined by author and by software (PISA)
Molecular Components in 5A7U
Label Count Molecule
Protein (1 molecule)
Regulatory Protein Adr1(Gene symbol: ADR1)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB