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Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA

080500226 添加于 2010-11-21 10:54 | 1835 次阅读 | 0 个评论

作者
Reiter NJ, Osterman A, Torres-Larios A, Swinger KK, Pan T, Mondragón A
摘要
Ribonuclease (RNase) P is the universal ribozyme responsible for 5′-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNAPhe. The 154 kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a mature tRNA. The structure shows that RNA–RNA recognition occurs through shape complementarity, specific intermolecular contacts and base-pairing interactions. Soaks with a pre-tRNA 5′ leader sequence with and without metal help to identify the 5′ substrate path and potential catalytic metal ions. The protein binds on top of a universally conserved structural module in P RNA and interacts with the leader, but not with the mature tRNA. The active site is composed of phosphate backbone moieties, a universally conserved uridine nucleobase, and at least two catalytically important metal ions. The active site structure and conserved RNase P–tRNA contacts suggest a universal mechanism of catalysis by RNase P.
详细资料
- 文献种类:期刊
- 期刊名称: Nature
- 期刊缩写: Nature
- 期卷页: 2010年
- ISBN: 0028-0836
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