2vnu
From Proteopedia
CRYSTAL STRUCTURE OF SC RRP44
Overview
The eukaryotic exosome is a macromolecular complex essential for RNA processing and decay. It has recently been shown that the RNase activity of the yeast exosome core can be mapped to a single subunit, Rrp44, which processively degrades single-stranded RNAs as well as RNAs containing secondary structures. Here we present the 2.3 A resolution crystal structure of S. cerevisiae Rrp44 in complex with single-stranded RNA. Although Rrp44 has a linear domain organization similar to bacterial RNase II, in three dimensions the domains have a different arrangement. The three domains of the classical nucleic-acid-binding OB fold are positioned on the catalytic domain such that the RNA-binding path observed in RNase II is occluded. Instead, RNA is threaded to the catalytic site via an alternative route suggesting a mechanism for RNA-duplex unwinding. The structure provides a molecular rationale for the observed biochemical properties of the RNase R family of nucleases.
About this Structure
2VNU is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family., Lorentzen E, Basquin J, Tomecki R, Dziembowski A, Conti E, Mol Cell. 2008 Mar 28;29(6):717-28. PMID:18374646
Categories: Protein complex | Saccharomyces cerevisiae | Basquin, J. | Conti, E. | Lorentzen, E. | Cytoplasm | Dis3p | Exonuclease | Exosome | Hydrolase | Nuclease | Nucleus | Rna degradation | Rna processing | Rna-binding | Rrna processing | Rrp44
