Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA.

Reiter NJ, Osterman A, Torres-Larios A, Swinger KK, Pan T, Mondragón A
Nature. 2010 468 (7325): 784-9

PMID: 21076397 · PMCID: PMC3058908 · DOI:10.1038/nature09516

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 tRNA(Phe). The 154‚ÄČkDa 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.

MeSH Terms (13)

Biocatalysis Catalytic Domain Crystallography, X-Ray Genes, Bacterial Holoenzymes Metals Models, Molecular Molecular Conformation Ribonuclease P RNA, Transfer, Phe Structure-Activity Relationship Substrate Specificity Thermotoga maritima

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