6H25

Human nuclear RNA exosome EXO-10-MPP6 complex

Summary for 6H25

• Entry DOI: 10.2210/pdb6h25/pdb
• EMDB information: 0127 0128
• Descriptor: Exosome complex component RRP45, Exosome complex exonuclease RRP44, M-phase phosphoprotein 6, ... (12 entities in total)
• Functional Keywords: nuclear exosome, rna decay, cryoem, hexo-10, hdis3, hmpp6, rna binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 421248.56

Authors

Gerlach, P.,Schuller, J.M.,Falk, S.,Basquin, J.,Conti, E. (deposition date: 2018-07-13, release date: 2018-08-15, Last modification date: 2024-05-15)

Primary citation

Gerlach, P.,Schuller, J.M.,Bonneau, F.,Basquin, J.,Reichelt, P.,Falk, S.,Conti, E.
Distinct and evolutionary conserved structural features of the human nuclear exosome complex.
Elife, 7:-, 2018

PubMed Abstract: The nuclear RNA exosome complex mediates the processing of structured RNAs and the decay of aberrant non-coding RNAs, an important function particularly in human cells. Most mechanistic studies to date have focused on the yeast system. Here, we reconstituted and studied the properties of a recombinant 14-subunit human nuclear exosome complex. In biochemical assays, the human exosome embeds a longer RNA channel than its yeast counterpart. The 3.8 Å resolution cryo-EM structure of the core complex bound to a single-stranded RNA reveals that the RNA channel path is formed by two distinct features of the hDIS3 exoribonuclease: an open conformation and a domain organization more similar to bacterial RNase II than to yeast Rrp44. The cryo-EM structure of the holo-complex shows how obligate nuclear cofactors position the hMTR4 helicase at the entrance of the core complex, suggesting a striking structural conservation from lower to higher eukaryotes.

PubMed: 30047866
DOI: 10.7554/eLife.38686

Experimental method

ELECTRON MICROSCOPY (3.8 Å)