7QDS

Apo human SKI complex in the open state

Summary for 7QDS

• Entry DOI: 10.2210/pdb7qds/pdb
• EMDB information: 13925
• Descriptor: Helicase SKI2W, Tetratricopeptide repeat protein 37, WD repeat-containing protein 61 (3 entities in total)
• Functional Keywords: multiprotein complex, rna helicase, dexh-box helicase, atpase, rna binding, rna binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 383800.26

Authors

Koegel, A.,Keidel, A.,Bonneau, A.,Schaefer, I.B.,Conti, E. (deposition date: 2021-11-30, release date: 2022-02-02, Last modification date: 2024-07-17)

Primary citation

Kogel, A.,Keidel, A.,Bonneau, F.,Schafer, I.B.,Conti, E.
The human SKI complex regulates channeling of ribosome-bound RNA to the exosome via an intrinsic gatekeeping mechanism.
Mol.Cell, 82:756-, 2022

PubMed Abstract: The superkiller (SKI) complex is the cytoplasmic co-factor and regulator of the RNA-degrading exosome. In human cells, the SKI complex functions mainly in co-translational surveillance-decay pathways, and its malfunction is linked to a severe congenital disorder, the trichohepatoenteric syndrome. To obtain insights into the molecular mechanisms regulating the human SKI (hSKI) complex, we structurally characterized several of its functional states in the context of 80S ribosomes and substrate RNA. In a prehydrolytic ATP form, the hSKI complex exhibits a closed conformation with an inherent gating system that effectively traps the 80S-bound RNA into the hSKI2 helicase subunit. When active, hSKI switches to an open conformation in which the gating is released and the RNA 3' end exits the helicase. The emerging picture is that the gatekeeping mechanism and architectural remodeling of hSKI underpin a regulated RNA channeling system that is mechanistically conserved among the cytoplasmic and nuclear helicase-exosome complexes.

PubMed: 35120588
DOI: 10.1016/j.molcel.2022.01.009

Experimental method

ELECTRON MICROSCOPY (3.8 Å)