6ah3 | pdb_00006ah3

Cryo-EM structure of yeast Ribonuclease P with pre-tRNA substrate

spinqualitylabelsall models 6ah3, resolution 3.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ah3 is a 12 chain structure with sequence from [1] and Saccharomyces cerevisiae (strain atcc 204508 / s288c). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, ZN Activity: Ribonuclease P, with EC number 3.1.26.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [POP6_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. [POP3_YEAST] Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA. [POP7_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. [RPP1_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. [POP1_YEAST] Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA. [POP8_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. [POP4_YEAST] Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P. [RPR2_YEAST] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [POP5_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. Publication Abstract from PubMed Ribonuclease 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA