EMD-9032

Single-particle
4.0 Å
EMD-9032 Deposition: 09/08/2018
Map released: 17/10/2018
Last modified: 29/05/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-9032

Full-length S. pombe Mdn1 in the presence of AMPPNP (ring region)

EMD-9032

Single-particle
4.0 Å
EMD-9032 Deposition: 09/08/2018
Map released: 17/10/2018
Last modified: 29/05/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Schizosaccharomyces pombe, Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Sample: N-terminal density map of the full-length Mdn1 in the presence of AMPPNP
Fitted models: 6or5 (Avg. Q-score: 0.409)

Deposition Authors: Chen Z, Suzuki H, Wang AC, DiMaio F, Walz T, Kapoor TM
Structural Insights into Mdn1, an Essential AAA Protein Required for Ribosome Biogenesis.
Chen Z , Suzuki H , Kobayashi Y , Wang AC , DiMaio F, Kawashima SA, Walz T , Kapoor TM
(2018) Cell , 175 , 822 - 834.e18
PUBMED: 30318141
DOI: doi:10.1016/j.cell.2018.09.015
ISSN: 1097-4172
Abstract:
Mdn1 is an essential AAA (ATPase associated with various activities) protein that removes assembly factors from distinct precursors of the ribosomal 60S subunit. However, Mdn1's large size (∼5,000 amino acid [aa]) and its limited homology to other well-studied proteins have restricted our understanding of its remodeling function. Here, we present structures for S. pombe Mdn1 in the presence of AMPPNP at up to ∼4 Å or ATP plus Rbin-1, a chemical inhibitor, at ∼8 Å resolution. These data reveal that Mdn1's MIDAS domain is tethered to its ring-shaped AAA domain through an ∼20 nm long structured linker and a flexible ∼500 aa Asp/Glu-rich motif. We find that the MIDAS domain, which also binds other ribosome-assembly factors, docks onto the AAA ring in a nucleotide state-specific manner. Together, our findings reveal how conformational changes in the AAA ring can be directly transmitted to the MIDAS domain and thereby drive the targeted release of assembly factors from ribosomal 60S-subunit precursors.