6I27

Rea1 AAA2L-H2alpha deletion mutant in AMPPNP State

Summary for 6I27

• Entry DOI: 10.2210/pdb6i27/pdb
• Related: 6HYD 6HYP
• EMDB information: 0308 0309 0329
• Descriptor: Midasin,Midasin,Midasin,Midasin,Midasin,Midasin,Midasin (1 entity in total)
• Functional Keywords: rea1, mdn1, midasin, aaa+ protein, ribosome maturation, molecular machine, motor protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 1
• Total formula weight: 546538.25

Authors

Sosnowski, P.,Urnavicius, L.,Boland, A.,Fagiewicz, R.,Busselez, J.,Papai, G.,Schmidt, H. (deposition date: 2018-10-31, release date: 2018-12-12, Last modification date: 2024-05-15)

Primary citation

Sosnowski, P.,Urnavicius, L.,Boland, A.,Fagiewicz, R.,Busselez, J.,Papai, G.,Schmidt, H.
The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1.
Elife, 7:-, 2018

PubMed Abstract: The biogenesis of 60S ribosomal subunits is initiated in the nucleus where rRNAs and proteins form pre-60S particles. These pre-60S particles mature by transiently interacting with various assembly factors. The ~5000 amino-acid AAA+ ATPase Rea1 (or Midasin) generates force to mechanically remove assembly factors from pre-60S particles, which promotes their export to the cytosol. Here we present three Rea1 cryoEM structures. We visualise the Rea1 engine, a hexameric ring of AAA+ domains, and identify an α-helical bundle of AAA2 as a major ATPase activity regulator. The α-helical bundle interferes with nucleotide-induced conformational changes that create a docking site for the substrate binding MIDAS domain on the AAA +ring. Furthermore, we reveal the architecture of the Rea1 linker, which is involved in force generation and extends from the AAA+ ring. The data presented here provide insights into the mechanism of one of the most complex ribosome maturation factors.

PubMed: 30460895
DOI: 10.7554/eLife.39163

Experimental method

ELECTRON MICROSCOPY (7.8 Å)