6OR6

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

6OR6 の概要

• エントリーDOI: 10.2210/pdb6or6/pdb
• EMDBエントリー: 9032 9033 9034 9035 9036
• 分子名称: Midasin (1 entity in total)
• 機能のキーワード: ribosome biogenesis, aaa protein, mechanochemical enzyme, ribosome assembly factor, motor protein
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 538381.13

構造登録者

Chen, Z.,Suzuki, H.,Wang, A.C.,DiMaio, F.,Walz, T.,Kapoor, T.M. (登録日: 2019-04-29, 公開日: 2019-05-29, 最終更新日: 2024-03-13)

主引用文献

Chen, Z.,Suzuki, H.,Kobayashi, Y.,Wang, A.C.,DiMaio, F.,Kawashima, S.A.,Walz, T.,Kapoor, T.M.
Structural Insights into Mdn1, an Essential AAA Protein Required for Ribosome Biogenesis.
Cell, 175:822-834.e18, 2018

PubMed 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.

PubMed: 30318141
DOI: 10.1016/j.cell.2018.09.015

実験手法

ELECTRON MICROSCOPY (5.3 Å)