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

Autor:	Scott A. Strobel, Mary R. Stahley
Rok vydání:	2005
Předmět:	Models Molecular Genetics Multidisciplinary Cations Divalent Stereochemistry RNA Splicing Group I intron splicing Intron Guanosine RNA Crystal structure Biology Ligands Introns Metal chemistry.chemical_compound Exon chemistry visual_art RNA splicing visual_art.visual_art_medium Magnesium RNA Catalytic
Zdroj:	Science. 309:1587-1590
ISSN:	1095-9203 0036-8075
DOI:	10.1126/science.1114994
Popis:	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 Mg 2+ 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a98dad812d966d24e5b02aa1d26c79b https://doi.org/10.1126/science.1114994 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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