5a7u

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

spinqualitylabelsall models 5a7u, resolution 4.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a7u is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ADR1_YEAST] Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2). Publication Abstract from PubMed 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. Cotranslational Protein Folding inside the Ribosome Exit Tunnel.,Nilsson OB, Hedman R, Marino J, Wickles S, Bischoff L, Johansson M, Muller-Lucks A, Trovato F, Puglisi JD, O'Brien EP, Beckmann R, von Heijne G Cell Rep. 2015 Sep 8;12(10):1533-40. doi: 10.1016/j.celrep.2015.07.065. Epub 2015, Aug 28. PMID:26321634 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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