2VNU

Crystal structure of Sc Rrp44

Summary for 2VNU

• Entry DOI: 10.2210/pdb2vnu/pdb
• Descriptor: 5'-R(*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP)-3', EXOSOME COMPLEX EXONUCLEASE RRP44, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: hydrolase-rna complex, rna degradation, rna-binding, rna processing, hydrolase/rna
• Biological source: SACCHAROMYCES CEREVISIAE (BAKERS YEAST); More
• Cellular location: Cytoplasm: Q08162
• Total number of polymer chains: 2
• Total formula weight: 90572.60

Authors

Lorentzen, E.,Basquin, J.,Conti, E. (deposition date: 2008-02-07, release date: 2008-04-08, Last modification date: 2024-11-06)

Primary citation

Lorentzen, E.,Basquin, J.,Tomecki, R.,Dziembowski, A.,Conti, E.
Structure of the Active Subunit of the Yeast Exosome Core, Rrp44: Diverse Modes of Substrate Recruitment in the Rnase II Nuclease Family
Mol.Cell, 29:717-, 2008

PubMed Abstract: 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.

PubMed: 18374646
DOI: 10.1016/J.MOLCEL.2008.02.018

Experimental method

X-RAY DIFFRACTION (2.3 Å)