2c39
From Proteopedia
RNASE PH CORE OF THE ARCHAEAL EXOSOME IN COMPLEX WITH ADP
Overview
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.
About this Structure
2C39 is a Protein complex structure of sequences from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core., Lorentzen E, Conti E, Mol Cell. 2005 Nov 11;20(3):473-81. PMID:16285928 Page seeded by OCA on Sat May 3 21:10:57 2008
Categories: Protein complex | Sulfolobus solfataricus | Conti, E. | Lorentzen, E. | Archaeal | Exonuclease | Exoribonuclease | Exosome | Hydrolase | Nuclease | Phosphorolytic | Rna degradation | Rnase ph | Rrp41 | Rrp42
