5JEA

Structure of a cytoplasmic 11-subunit RNA exosome complex including Ski7, bound to RNA

Summary for 5JEA

• Entry DOI: 10.2210/pdb5jea/pdb
• Descriptor: Exosome complex component RRP45, Exosome complex exonuclease DIS3, Superkiller protein 7,Endolysin, ... (16 entities in total)
• Functional Keywords: exosome, ski7, nuclease, rna degradation, hydrolase- rna complex, hydrolase-rna complex, hydrolase/rna
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Cellular location: Cytoplasm : Q05636 Q08162 P46948 P25359 P53256 Q12277 P48240 Q08285 P38792 P53859; Host cytoplasm : P00720
• Total number of polymer chains: 12
• Total formula weight: 442281.06

Authors

Kowalinski, E.,Ebert, J.,Stegmann, E.,Conti, E. (deposition date: 2016-04-18, release date: 2016-07-13, Last modification date: 2024-01-10)

Primary citation

Kowalinski, E.,Kogel, A.,Ebert, J.,Reichelt, P.,Stegmann, E.,Habermann, B.,Conti, E.
Structure of a Cytoplasmic 11-Subunit RNA Exosome Complex.
Mol.Cell, 63:125-134, 2016

PubMed Abstract: The RNA exosome complex associates with nuclear and cytoplasmic cofactors to mediate the decay, surveillance, or processing of a wide variety of transcripts. In the cytoplasm, the conserved core of the exosome (Exo10) functions together with the conserved Ski complex. The interaction of S. cerevisiae Exo10 and Ski is not direct but requires a bridging cofactor, Ski7. Here, we report the 2.65 Å resolution structure of S. cerevisiae Exo10 bound to the interacting domain of Ski7. Extensive hydrophobic interactions rationalize the high affinity and stability of this complex, pointing to Ski7 as a constitutive component of the cytosolic exosome. Despite the absence of sequence homology, cytoplasmic Ski7 and nuclear Rrp6 bind Exo10 using similar surfaces and recognition motifs. Knowledge of the interacting residues in the yeast complexes allowed us to identify a splice variant of human HBS1-Like as a Ski7-like exosome-binding protein, revealing the evolutionary conservation of this cytoplasmic cofactor.

PubMed: 27345150
DOI: 10.1016/j.molcel.2016.05.028

Experimental method

X-RAY DIFFRACTION (2.65 Å)