2BR2

RNase PH core of the archaeal exosome

Summary for 2BR2

• Entry DOI: 10.2210/pdb2br2/pdb
• Descriptor: EXOSOME COMPLEX EXONUCLEASE 2, EXOSOME COMPLEX EXONUCLEASE 1, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: exosome, rnase ph, phosphorolytic, exoribonuclease, rna degradation, archaeal, hydrolase
• Biological source: SULFOLOBUS SOLFATARICUS; More
• Cellular location: Cytoplasm (Potential): Q9UXC0 Q9UXC2
• Total number of polymer chains: 24
• Total formula weight: 694547.62

Authors

lorentzen, E.,Fribourg, S.,Conti, E. (deposition date: 2005-04-30, release date: 2005-06-06, Last modification date: 2023-12-13)

Primary citation

Lorentzen, E.,Walter, P.,Fribourg, S.,Evguenieva-Hackenberg, E.,Klug, G.,Conti, E.
The Archaeal Exosome Core is a Hexameric Ring Structure with Three Catalytic Subunits.
Nat.Struct.Mol.Biol., 12:575-, 2005

PubMed Abstract: The exosome is a 3' --> 5' exoribonuclease complex involved in RNA processing. We report the crystal structure of the RNase PH core complex of the Sulfolobus solfataricus exosome determined at a resolution of 2.8 A. The structure reveals a hexameric ring-like arrangement of three Rrp41-Rrp42 heterodimers, where both subunits adopt the RNase PH fold common to phosphorolytic exoribonucleases. Structure-guided mutagenesis reveals that the activity of the complex resides within the active sites of the Rrp41 subunits, all three of which face the same side of the hexameric structure. The Rrp42 subunit is inactive but contributes to the structuring of the Rrp41 active site. The high sequence similarity of this archaeal exosome to eukaryotic exosomes and its high structural similarity to the bacterial mRNA-degrading PNPase support a common basis for RNA-degrading machineries in all three domains of life.

PubMed: 15951817
DOI: 10.1038/NSMB952

Experimental method

X-RAY DIFFRACTION (2.8 Å)