1UOC

X-ray structure of the RNase domain of the yeast Pop2 protein

Summary for 1UOC

• Entry DOI: 10.2210/pdb1uoc/pdb
• Descriptor: POP2, CALCIUM ION, XENON, ... (4 entities in total)
• Functional Keywords: hydrolase, dedd nuclease, mrna degradation, poly(a) tail, transcription regulation, repressor, phosphorylation.
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Cytoplasm: P39008
• Total number of polymer chains: 2
• Total formula weight: 67031.93

Authors

Thore, S.,Mauxion, F.,Seraphin, B.,Suck, D. (deposition date: 2003-09-16, release date: 2003-11-20, Last modification date: 2024-05-08)

Primary citation

Thore, S.,Mauxion, F.,Seraphin, B.,Suck, D.
X-Ray Structure and Activity of the Yeast Pop2 Protein: A Nuclease Subunit of the Mrna Deadenylase Complex
Embo Rep., 4:1150-, 2003

PubMed Abstract: In Saccharomyces cerevisiae, a large complex, known as the Ccr4-Not complex, containing two nucleases, is responsible for mRNA deadenylation. One of these nucleases is called Pop2 and has been identified by similarity with PARN, a human poly(A) nuclease. Here, we present the crystal structure of the nuclease domain of Pop2 at 2.3 A resolution. The domain has the fold of the DnaQ family and represents the first structure of an RNase from the DEDD superfamily. Despite the presence of two non-canonical residues in the active site, the domain displays RNase activity on a broad range of RNA substrates. Site-directed mutagenesis of active-site residues demonstrates the intrinsic ability of the Pop2 RNase D domain to digest RNA. This first structure of a nuclease involved in the 3'-5' deadenylation of mRNA in yeast provides information for the understanding of the mechanism by which the Ccr4-Not complex achieves its functions.

PubMed: 14618157
DOI: 10.1038/SJ.EMBOR.7400020

Experimental method

X-RAY DIFFRACTION (2.3 Å)