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Science 2 September 2005:
Vol. 309. no. 5740, pp. 1587 - 1590
DOI: 10.1126/science.1114994
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Reports

Structural Evidence for a Two-Metal-Ion Mechanism of Group I Intron Splicing

Mary R. Stahley and Scott A. Strobel*

We report the 3.4 angstrom crystal structure of a catalytically active group I intron splicing intermediate containing the complete intron, both exons, the scissile phosphate, and all of the functional groups implicated in catalytic metal ion coordination, including the 2'-OH of the terminal guanosine. This structure suggests that, like protein phosphoryltransferases, an RNA phosphoryltransferase can use a two-metal-ion mechanism. Two Mg2+ ions are positioned 3.9 angstroms apart and are directly coordinated by all six of the biochemically predicted ligands. The evolutionary convergence of RNA and protein active sites on the same inorganic architecture highlights the intrinsic chemical capacity of the two-metal-ion catalytic mechanism for phosphoryl transfer.

Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, New Haven, CT 06520-8114, USA.

* To whom correspondence should be addressed. E-mail: scott.strobel{at}yale.edu

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