2NN6

Structure of the human RNA exosome composed of Rrp41, Rrp45, Rrp46, Rrp43, Mtr3, Rrp42, Csl4, Rrp4, and Rrp40

Summary for 2NN6

• Entry DOI: 10.2210/pdb2nn6/pdb
• Descriptor: Polymyositis/scleroderma autoantigen 1, Exosome complex exonuclease RRP41, Exosome complex exonuclease RRP43, ... (9 entities in total)
• Functional Keywords: rna, exosome, pm/scl, exoribonuclease, phosphorolytic, ribonuclease, hydrolase-transferase complex, hydrolase/transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q9NPD3 Q96B26 Q9NQT5 Q13868; Nucleus, nucleolus: Q9NQT4 Q15024 Q9Y3B2; Cytoplasm (Probable): Q5RKV6
• Total number of polymer chains: 9
• Total formula weight: 272665.69

Authors

Lima, C.D. (deposition date: 2006-10-23, release date: 2006-12-26, Last modification date: 2023-12-27)

Primary citation

Liu, Q.,Greimann, J.C.,Lima, C.D.
Reconstitution, activities, and structure of the eukaryotic RNA exosome.
Cell(Cambridge,Mass.), 127:1223-1237, 2006

PubMed Abstract: The RNA exosome is a multisubunit 3' to 5' exoribonuclease complex that participates in degradation and processing of cellular RNA. To determine the activities and structure of the eukaryotic exosome, we report the reconstitution of 9-subunit exosomes from yeast and human and reconstitution of 10- and 11-subunit exosomes from yeast. Comparative biochemical analysis between purified subunits and reconstituted exosomes using AU-rich, polyadenylated (poly[A]), generic, and structured RNA substrates reveals processive phosphorolytic activities for human Rrp41/Rrp45 and the 9-subunit human exosome, processive hydrolytic activities for yeast Rrp44 and the yeast 10-subunit exosome, distributive hydrolytic activities for Rrp6, and processive and distributive hydrolytic activities for the yeast 11-subunit exosome. To elucidate the architecture of a eukaryotic exosome, its conserved surfaces, and the structural basis for RNA decay, we report the X-ray structure determination for the 286 kDa nine-subunit human exosome at 3.35 A.

PubMed: 17174896
DOI: 10.1016/j.cell.2006.10.037

Experimental method

X-RAY DIFFRACTION (3.35 Å)