6k0b | pdb_00006k0b

cryo-EM structure of archaeal Ribonuclease P with mature tRNA

spinqualitylabelsall models 6k0b, resolution 4.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6k0b is a 14 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 6k0a Activity: Ribonuclease P, with EC number 3.1.26.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RNP4_METJA] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.[HAMAP-Rule:MF_00757] [RNP2_METJA] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.[HAMAP-Rule:MF_00755] [RNP1_METJA] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.[HAMAP-Rule:MF_00754] [RNP3_METJA] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.[HAMAP-Rule:MF_00756] [RL7A_METJA] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs. Publication Abstract from PubMed Ribonuclease P (RNase P) is an essential ribozyme responsible for tRNA 5' maturation. Here we report the cryo-EM structures of Methanocaldococcus jannaschii (Mja) RNase P holoenzyme alone and in complex with a tRNA substrate at resolutions of 4.6 A and 4.3 A, respectively. The structures reveal that the subunits of MjaRNase P are strung together to organize the holoenzyme in a dimeric conformation required for efficient catalysis. The structures also show that archaeal RNase P is a functional chimera of bacterial and eukaryal RNase Ps that possesses bacterial-like two RNA-based anchors and a eukaryal-like protein-aided stabilization mechanism. The 3'-RCCA sequence of tRNA, which is a key recognition element for bacterial RNase P, is dispensable for tRNA recognition by MjaRNase P. The overall organization of MjaRNase P, particularly within the active site, is similar to those of bacterial and eukaryal RNase Ps, suggesting a universal catalytic mechanism for all RNase Ps. Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.,Wan F, Wang Q, Tan J, Tan M, Chen J, Shi S, Lan P, Wu J, Lei M Nat Commun. 2019 Jun 13;10(1):2617. doi: 10.1038/s41467-019-10496-3. PMID:31197137 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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