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Crystallization and preliminary crystallographic studies of putative RNA 3'-terminal phosphate cyclase from the crenarchaeon Sulfolobus tokodaii



Crystallization and preliminary crystallographic studies of putative RNA 3'-terminal phosphate cyclase from the crenarchaeon Sulfolobus tokodaii



Acta Crystallographica. Section F Structural Biology and Crystallization Communications 65(Pt 6): 565-570



RNA 3'-terminal phosphate cyclase (Rtc) is an enzyme involved in RNA splicing that converts the 3'-terminal hydroxyl group of truncated RNA to 2',3'-cyclic phosphate, which is required just before its ligation. This reaction may occur in the following two steps: (i) Rtc + ATP --> Rtc-AMP + PP(i) and (ii) RNA-N3'p + Rtc-AMP --> RNA-N>p + Rtc + AMP. In order to reveal the reaction mechanism, Rtc of Sulfolobus tokodaii (St-Rtc) overexpressed in Escherichia coli was purified and crystallized in the following states: St-Rtc, St-Rtc+Mn, St-Rtc+ATP, St-Rtc+AMP and St-Rtc-AMP. The crystals diffracted to 2.25-3.00 A resolution and preliminary solutions of their structures have been obtained by molecular replacement using the structure of a selenomethionine-labelled St-Rtc crystal which was solved in advance using the MAD method as a model. These crystals grew in two different space groups (P3(1) and P4(2)), with the former space group displaying two distinct packing modes.

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Accession: 052399346

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PMID: 19478432

DOI: 10.1107/s1744309109014663


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