"Structural organization of box C/D RNA-guided RNA methyltransferase."
Ye K, Jia R, Lin J, Ju M, Peng J, Xu A, Zhang L
Published 2009-08-18 in Proc Natl Acad Sci U S A volume 106 .
Pubmed ID: 19666563
DOI identifier: -
|Box C/D guide RNAs are abundant noncoding RNAs that primarily function to direct the 2'-O-methylation of specific nucleotides by base-pairing with substrate RNAs. In archaea, a bipartite C/D RNA assembles with L7Ae, Nop5, and the methyltransferase fibrillarin into a modification enzyme with unique substrate specificity. Here, we determined the crystal structure of an archaeal C/D RNA-protein complex (RNP) composed of all 3 core proteins and an engineered half-guide RNA at 4 A resolution, as well as 2 protein substructures at higher resolution. The RNP structure reveals that the C-terminal domains of Nop5 in the dimeric complex provide symmetric anchoring sites for 2 L7Ae-associated kink-turn motifs of the C/D RNA. A prominent protrusion in Nop5 seems to be important for guide RNA organization and function and for discriminating the structurally related U4 snRNA. Multiple conformations of the N-terminal domain of Nop5 and its associated fibrillarin in different structures indicate the inherent flexibility of the catalytic module, suggesting that a swinging motion of the catalytic module is part of the enzyme mechanism. We also built a model of a native C/D RNP with substrate and fibrillarin in an active conformation. Our results provide insight into the overall organization and mechanism of action of C/D RNA-guided RNA methyltransferases.|
This publication refers to following proteins:
- FlpA (Sulfolobus solfataricus)
- L7Ae (Sulfolobus solfataricus)
- Nop56/58 (Sulfolobus solfataricus)
Last modification of this entry: Sept. 6, 2012