5OKZ

Crystal Strucrure of the Mpp6 Exosome complex

Summary for 5OKZ

• Entry DOI: 10.2210/pdb5okz/pdb
• Descriptor: Exosome complex component CSL4, M-phase phosphoprotein 6 homolog, TRIS(HYDROXYETHYL)AMINOMETHANE, ... (14 entities in total)
• Functional Keywords: rna degradation exosome ribosome biogenesis kh-domain, rna binding protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Cellular location: Cytoplasm : P53859 Q05636 P46948 P25359 P53256 Q12277 P48240 Q08285 P38792; Nucleus : P53725
• Total number of polymer chains: 40
• Total formula weight: 1211381.84

Authors

Falk, S.,Ebert, J.,Conti, E. (deposition date: 2017-07-26, release date: 2017-08-30, Last modification date: 2024-11-13)

Primary citation

Falk, S.,Bonneau, F.,Ebert, J.,Kogel, A.,Conti, E.
Mpp6 Incorporation in the Nuclear Exosome Contributes to RNA Channeling through the Mtr4 Helicase.
Cell Rep, 20:2279-2286, 2017

PubMed Abstract: The RNA-degrading exosome mediates the processing and decay of many cellular transcripts. In the yeast nucleus, the ubiquitous 10-subunit exosome core complex (Exo-9-Rrp44) functions with four conserved cofactors (Rrp6, Rrp47, Mtr4, and Mpp6). Biochemical and structural studies to date have shed insights into the mechanisms of the exosome core and its nuclear cofactors, with the exception of Mpp6. We report the 3.2-Å resolution crystal structure of a S. cerevisiae Exo-9-Mpp6 complex, revealing how linear motifs in the Mpp6 middle domain bind Rrp40 via evolutionary conserved residues. In particular, Mpp6 binds near a tryptophan residue of Rrp40 that is mutated in human patients suffering from pontocerebellar hypoplasia. Using biochemical assays, we show that Mpp6 is required for the ability of Mtr4 to extend the trajectory of an RNA entering the exosome core, suggesting that it promotes the channeling of substrates from the nuclear helicase to the processive RNase.

PubMed: 28877463
DOI: 10.1016/j.celrep.2017.08.033

Experimental method

X-RAY DIFFRACTION (3.20003898551 Å)