2C37

RNASE PH CORE OF THE ARCHAEAL EXOSOME IN COMPLEX WITH U8 RNA

Summary for 2C37

• Entry DOI: 10.2210/pdb2c37/pdb
• Related: 2BR2 2C38 2C39
• Descriptor: PROBABLE EXOSOME COMPLEX EXONUCLEASE 2, PROBABLE EXOSOME COMPLEX EXONUCLEASE 1, URIDINE-5'-MONOPHOSPHATE, ... (6 entities in total)
• Functional Keywords: exosome, rrp41, rrp42, exoribonuclease, rna degradation, archaeal, hydrolase
• Biological source: SULFOLOBUS SOLFATARICUS; More
• Total number of polymer chains: 24
• Total formula weight: 702869.79

Authors

Lorentzen, E.,Conti, E. (deposition date: 2005-10-04, release date: 2005-11-23, Last modification date: 2023-12-13)

Primary citation

Lorentzen, E.,Conti, E.
Structural Basis of 3' End RNA Recognition and Exoribonucleolytic Cleavage by an Exosome Rnase Ph Core.
Mol.Cell, 20:473-, 2005

PubMed Abstract: The exosome is a macromolecular complex that plays fundamental roles in the biogenesis and turnover of a large number of RNA species. Here we report the crystal structures of the Rrp41-Rrp42 core complex of the S. solfataricus exosome bound to short single-stranded RNAs and to ADP. The RNA binding cleft recognizes four nucleotides in a sequence-unspecific manner, mainly by electrostatic interactions with the phosphate groups. Interactions at the 2' hydroxyls of the sugars provide specificity for RNA over DNA. The structures show both the bound substrate and the cleaved product of the reaction, suggesting a catalytic mechanism for the 3'-5' phosphorolytic activity of the exosome.

PubMed: 16285928
DOI: 10.1016/J.MOLCEL.2005.10.020

Experimental method

X-RAY DIFFRACTION (2.8 Å)