6ah3
Cryo-EM structure of yeast Ribonuclease P with pre-tRNA substrate
Structural highlights
FunctionPOP6_YEAST Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.[1] Publication Abstract from PubMedRibonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-tRNA. Here we report the 3.5-A cryo-EM structures of Saccharomyces cerevisiae RNase P alone and in complex with pre-tRNA(Phe) The protein components form a hook-shaped architecture that wraps around the RNA and stabilizes RNase P into a "measuring device" with two fixed anchors that recognize the L-shaped pre-tRNA. A universally conserved uridine nucleobase and phosphate backbone in the catalytic center together with the scissile phosphate and the O3' leaving group of pre-tRNA jointly coordinate two catalytic magnesium ions. Binding of pre-tRNA induces a conformational change in the catalytic center that is required for catalysis. Moreover, simulation analysis suggests a two-metal-ion SN2 reaction pathway of pre-tRNA cleavage. These results not only reveal the architecture of yeast RNase P but also provide a molecular basis of how the 5'-leader of pre-tRNA is processed by eukaryotic RNase P. Structural insight into precursor tRNA processing by yeast ribonuclease P.,Lan P, Tan M, Zhang Y, Niu S, Chen J, Shi S, Qiu S, Wang X, Peng X, Cai G, Cheng H, Wu J, Li G, Lei M Science. 2018 Sep 27. pii: science.aat6678. doi: 10.1126/science.aat6678. PMID:30262633[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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