2WP8

yeast rrp44 nuclease

Summary for 2WP8

• Entry DOI: 10.2210/pdb2wp8/pdb
• Related: 2VNU
• Descriptor: EXOSOME COMPLEX COMPONENT RRP45, EXOSOME COMPLEX COMPONENT SKI6, EXOSOME COMPLEX EXONUCLEASE DIS3, ... (5 entities in total)
• Functional Keywords: exosome, nucleus, nuclease, hydrolase, rna-binding, exonuclease, rna binding, mitochondrion, rrna processing
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm: Q05636 P46948 Q08162
• Total number of polymer chains: 3
• Total formula weight: 172970.73

Authors

Basquin, J.,Bonneau, F.,Ebert, J.,Lorentzen, E.,Conti, E. (deposition date: 2009-08-03, release date: 2009-11-10, Last modification date: 2024-11-06)

Primary citation

Bonneau, F.,Basquin, J.,Ebert, J.,Lorentzen, E.,Conti, E.
The Yeast Exosome Functions as a Macromolecular Cage to Channel RNA Substrates for Degradation.
Cell(Cambridge,Mass.), 139:547-, 2009

PubMed Abstract: The exosome is a conserved macromolecular complex essential for RNA degradation. The nine-subunit core of the eukaryotic exosome shares a similar barrel-like architecture with prokaryotic complexes, but is catalytically inert. Here, we investigate how the Rrp44 nuclease functions in the active ten-subunit exosome. The 3.0 A resolution crystal structure of the yeast Rrp44-Rrp41-Rrp45 complex shows how the nuclease interacts with the exosome core and the relative accessibility of its endoribonuclease and exoribonuclease sites. Biochemical studies indicate that RNAs thread through the central channel of the core to reach the Rrp44 exoribonuclease site. This channeling mechanism involves evolutionary conserved residues. It allows the processive unwinding and degradation of RNA duplexes containing a sufficiently long single-stranded 3' extension, without the requirement for helicase activities. Although the catalytic function of the exosome core has been lost during evolution, the substrate recruitment and binding properties have been conserved from prokaryotes to eukaryotes.

PubMed: 19879841
DOI: 10.1016/J.CELL.2009.08.042

Experimental method

X-RAY DIFFRACTION (3 Å)