6AGB
Cryo-EM structure of yeast Ribonuclease P
Summary for 6AGB
Entry DOI | 10.2210/pdb6agb/pdb |
EMDB information | 9616 |
Descriptor | Ribonuclease P RNA, Ribonuclease P protein subunit RPR2, ZINC ION, ... (11 entities in total) |
Functional Keywords | ribonuclease p, rna-protein complex, hydrolase-rna complex, hydrolase/rna |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Total number of polymer chains | 11 |
Total formula weight | 425186.39 |
Authors | |
Primary citation | 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. Structural insight into precursor tRNA processing by yeast ribonuclease P. Science, 362:-, 2018 Cited by PubMed Abstract: Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo-electron microscopy structures of RNase P alone and in complex with pre-tRNA 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 S2 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. PubMed: 30262633DOI: 10.1126/science.aat6678 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.48 Å) |
Structure validation
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