1uoc
From Proteopedia
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Revision as of 15:02, 5 November 2007
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X-RAY STRUCTURE OF THE RNASE DOMAIN OF THE YEAST POP2 PROTEIN
Overview
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.
About this Structure
1UOC is a Single protein structure of sequence from Saccharomyces cerevisiae with CA and XE as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex., Thore S, Mauxion F, Seraphin B, Suck D, EMBO Rep. 2003 Dec;4(12):1150-5. Epub 2003 Nov 14. PMID:14618157
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