7Z11

Structure of substrate bound DRG1 (AFG2)

Summary for 7Z11

• Entry DOI: 10.2210/pdb7z11/pdb
• EMDB information: 14437
• Descriptor: ATPase family gene 2 protein, peptide substrate, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total)
• Functional Keywords: ribosome biogenesis, aaa-atpases, substrate recognition, single particle cryo-em, chaperone
• Biological source: Saccharomyces cerevisiae S288C; More
• Total number of polymer chains: 7
• Total formula weight: 516580.14

Authors

Prattes, M.,Grishkovskaya, I.,Bergler, H.,Haselbach, D. (deposition date: 2022-02-24, release date: 2022-09-21, Last modification date: 2024-07-17)

Primary citation

Prattes, M.,Grishkovskaya, I.,Hodirnau, V.V.,Hetzmannseder, C.,Zisser, G.,Sailer, C.,Kargas, V.,Loibl, M.,Gerhalter, M.,Kofler, L.,Warren, A.J.,Stengel, F.,Haselbach, D.,Bergler, H.
Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1.
Nat.Struct.Mol.Biol., 29:942-953, 2022

PubMed Abstract: The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that initiates cytoplasmic maturation of the large ribosomal subunit. Drg1 releases the shuttling maturation factor Rlp24 from pre-60S particles shortly after nuclear export, a strict requirement for downstream maturation. The molecular mechanism of release remained elusive. Here, we report a series of cryo-EM structures that captured the extraction of Rlp24 from pre-60S particles by Saccharomyces cerevisiae Drg1. These structures reveal that Arx1 and the eukaryote-specific rRNA expansion segment ES27 form a joint docking platform that positions Drg1 for efficient extraction of Rlp24 from the pre-ribosome. The tips of the Drg1 N domains thereby guide the Rlp24 C terminus into the central pore of the Drg1 hexamer, enabling extraction by a hand-over-hand translocation mechanism. Our results uncover substrate recognition and processing by Drg1 step by step and provide a comprehensive mechanistic picture of the conserved modus operandi of AAA-ATPases.

PubMed: 36097293
DOI: 10.1038/s41594-022-00832-5

Experimental method

ELECTRON MICROSCOPY (3.2 Å)