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2i7x

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Revision as of 10:03, 21 November 2007 by OCA (Talk | contribs)
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2i7x, resolution 2.50Å

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Structure of Yeast CPSF-100 (Ydh1p)

Overview

Most eukaryotic messenger RNA precursors (pre-mRNAs) undergo extensive, maturational processing, including cleavage and polyadenylation at the, 3'-end. Despite the characterization of many proteins that are required, for the cleavage reaction, the identity of the endonuclease is not known., Recent analyses indicated that the 73-kDa subunit of cleavage and, polyadenylation specificity factor (CPSF-73) might be the endonuclease for, this and related reactions, although no direct data confirmed this. Here, we report the crystal structures of human CPSF-73 at 2.1 A resolution, complexed with zinc ions and a sulphate that might mimic the phosphate, group of the substrate, and the related yeast protein CPSF-100 (Ydh1) at, 2.5 A resolution. Both CPSF-73 and CPSF-100 contain two domains, a, metallo-beta-lactamase domain and a novel beta-CASP (named for, metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. The active site, of CPSF-73, with two zinc ions, is located at the interface of the two, domains. Purified recombinant CPSF-73 possesses RNA endonuclease activity, and mutations that disrupt zinc binding in the active site abolish this, activity. Our studies provide the first direct experimental evidence that, CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.

About this Structure

2I7X is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease., Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley JL, Tong L, Nature. 2006 Dec 14;444(7121):953-6. Epub 2006 Nov 26. PMID:17128255

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