3q1r
Crystal structure of a bacterial RNase P holoenzyme in complex with TRNA and in the presence of 5' leaderCrystal structure of a bacterial RNase P holoenzyme in complex with TRNA and in the presence of 5' leader
Structural highlights
Function[RNPA_THEMA] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme (By similarity). Publication Abstract from PubMedRibonuclease (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 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. Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA.,Reiter NJ, Osterman A, Torres-Larios A, Swinger KK, Pan T, Mondragon A Nature. 2010 Nov 14. PMID:21076397[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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