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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 catalyticallyactive group I intron splicing intermediate containing the completeintron, both exons, the scissile phosphate, and all of the functionalgroups implicated in catalytic metal ion coordination, includingthe 2'-OH of the terminal guanosine. This structure suggeststhat, like protein phosphoryltransferases, an RNA phosphoryltransferasecan use a two-metal-ion mechanism. Two Mg2+ ions are positioned3.9 angstroms apart and are directly coordinated by all sixof the biochemically predicted ligands. The evolutionary convergenceof RNA and protein active sites on the same inorganic architecturehighlights the intrinsic chemical capacity of the two-metal-ioncatalytic 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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