5DJE

Crystal structure of the zuotin homology domain (ZHD) from yeast Zuo1

Summary for 5DJE

• Entry DOI: 10.2210/pdb5dje/pdb
• Descriptor: Zuotin, DI(HYDROXYETHYL)ETHER, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: hsp-40, j-protein, molecular chaperone, ribomsome association, chaperone
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 34214.49

Authors

Shrestha, O.K.,Bingman, C.A.,Craig, E.A. (deposition date: 2015-09-02, release date: 2016-09-28, Last modification date: 2024-11-20)

Primary citation

Lee, K.,Sharma, R.,Shrestha, O.K.,Bingman, C.A.,Craig, E.A.
Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.
Nat.Struct.Mol.Biol., 23:1003-1010, 2016

PubMed Abstract: Ribosome-associated J protein-Hsp70 chaperones promote nascent-polypeptide folding and normal translational fidelity. The J protein Zuo1 is known to span the ribosomal subunits, but understanding of its function is limited. Here we present new structural and cross-linking data allowing more precise positioning of Saccharomyces cerevisiae Zuo1 near the 60S polypeptide-exit site and suggesting interactions of Zuo1 with the ribosomal protein eL31 and 25S rRNA helix 24. The junction between the 60S-interacting and subunit-spanning helices is a hinge that positions Zuo1 on the 40S yet accommodates subunit rotation. Interaction between the Zuo1 C terminus and 40S occurs via 18S rRNA expansion segment 12 (ES12) of helix 44, which originates at the decoding site. Deletions in either ES12 or the Zuo1 C terminus alter readthrough of stop codons and -1 frameshifting. Our study offers insight into how this cotranslational chaperone system may monitor decoding-site activity and nascent-polypeptide transit, thereby coordinating protein translation and folding.

PubMed: 27669034
DOI: 10.1038/nsmb.3299

Experimental method

X-RAY DIFFRACTION (1.85 Å)