5A7U

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

Summary for 5A7U

• Entry DOI: 10.2210/pdb5a7u/pdb
• EMDB information: 3079
• Descriptor: REGULATORY PROTEIN ADR1, ZINC ION (2 entities in total)
• Functional Keywords: protein folding, translation, ribosome, zinc finger, secm, translational arrest peptide, cryo-em, single- molecule studies
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: P07248
• Total number of polymer chains: 1
• Total formula weight: 3471.43

Authors

Nilsson, O.B.,Hedman, R.,Marino, J.,Wickles, S.,Bischoff, L.,Johansson, M.,Muller-Lucks, A.,Trovato, F.,Puglisi, J.D.,O'Brien, E.,Beckmann, R.,von Heijne, G. (deposition date: 2015-07-10, release date: 2015-09-16, Last modification date: 2024-05-08)

Primary citation

Nilsson, O.B.,Hedman, R.,Marino, J.,Wickles, S.,Bischoff, L.,Johansson, M.,Muller-Lucks, A.,Trovato, F.,Puglisi, J.D.,O'Brien, E.P.,Beckmann, R.,Von Heijne, G.
Cotranslational Protein Folding Inside the Ribosome Exit Tunnel.
Cell Rep., 12:1533-, 2015

PubMed Abstract: 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.

PubMed: 26321634
DOI: 10.1016/J.CELREP.2015.07.065

Experimental method

ELECTRON MICROSCOPY (4.8 Å)