Structural highlights
Publication Abstract from PubMed
Rix7 is an essential type II AAA-ATPase required for the formation of the large ribosomal subunit. Rix7 has been proposed to utilize the power of ATP hydrolysis to drive the removal of assembly factors from pre-60S particles, but the mechanism of release is unknown. Rix7's mammalian homolog, NVL2 has been linked to cancer and mental illness disorders, highlighting the need to understand the molecular mechanisms of this essential machine. Here we report the cryo-EM reconstruction of the tandem AAA domains of Rix7 which form an asymmetric stacked homohexameric ring. We trapped Rix7 with a polypeptide in the central channel, revealing Rix7's role as a molecular unfoldase. The structure establishes that type II AAA-ATPases lacking the aromatic-hydrophobic motif within the first AAA domain can engage a substrate throughout the entire central channel. The structure also reveals that Rix7 contains unique post-alpha7 insertions within both AAA domains important for Rix7 function.
Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7.,Lo YH, Sobhany M, Hsu AL, Ford BL, Krahn JM, Borgnia MJ, Stanley RE Nat Commun. 2019 Jan 31;10(1):513. doi: 10.1038/s41467-019-08373-0. PMID:30705282[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lo YH, Sobhany M, Hsu AL, Ford BL, Krahn JM, Borgnia MJ, Stanley RE. Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7. Nat Commun. 2019 Jan 31;10(1):513. doi: 10.1038/s41467-019-08373-0. PMID:30705282 doi:http://dx.doi.org/10.1038/s41467-019-08373-0
