PMID:10673421

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Citation

Palm, GJ, Billy, E, Filipowicz, W and Wlodawer, A (2000) Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology. Structure 8:13-23

Abstract

RNA cyclases are a family of RNA-modifying enzymes that are conserved in eucarya, bacteria and archaea. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. These enzymes might be responsible for production of the cyclic phosphate RNA ends that are known to be required by many RNA ligases in both prokaryotes and eukaryotes.

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Keywords

Amino Acid Sequence; Animals; Catalytic Domain; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Humans; Ligases/chemistry; Ligases/genetics; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Static Electricity

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