7f3e | pdb_00007f3e

Cryo-EM structure of the minimal protein-only RNase P from Aquifex aeolicus

spinqualitylabelsall models 7f3e, resolution 3.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7f3e is a 12 chain structure with sequence from Aquae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: aq_880 (AQUAE) Activity: Ribonuclease P, with EC number 3.1.26.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RFRNP_AQUAE] RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.[HAMAP-Rule:MF_01078] Publication Abstract from PubMed Ribonuclease P (RNase P) is an endoribonuclease that catalyzes the processing of the 5' leader sequence of precursor tRNA (pre-tRNA). Ribonucleoprotein RNase P and protein-only RNase P (PRORP) in eukaryotes have been extensively studied, but the mechanism by which a prokaryotic nuclease recognizes and cleaves pre-tRNA is unclear. To gain insights into this mechanism, we studied homologs of Aquifex RNase P (HARPs), thought to be enzymes of approximately 23 kDa comprising only this nuclease domain. We determined the cryo-EM structure of Aq880, the first identified HARP enzyme. The structure unexpectedly revealed that Aq880 consists of both the nuclease and protruding helical (PrH) domains. Aq880 monomers assemble into a dimer via the PrH domain. Six dimers form a dodecamer with a left-handed one-turn superhelical structure. The structure also revealed that the active site of Aq880 is analogous to that of eukaryotic PRORPs. The pre-tRNA docking model demonstrated that 5' processing of pre-tRNAs is achieved by two adjacent dimers within the dodecamer. One dimer is responsible for catalysis, and the PrH domains of the other dimer are responsible for pre-tRNA elbow recognition. Our study suggests that HARPs measure an invariant distance from the pre-tRNA elbow to cleave the 5' leader sequence, which is analogous to the mechanism of eukaryotic PRORPs and the ribonucleoprotein RNase P. Collectively, these findings shed light on how different types of RNase P enzymes utilize the same pre-tRNA processing. Minimal protein-only RNase P structure reveals insights into tRNA precursor recognition and catalysis.,Teramoto T, Koyasu T, Adachi N, Kawasaki M, Moriya T, Numata T, Senda T, Kakuta Y J Biol Chem. 2021 Sep;297(3):101028. doi: 10.1016/j.jbc.2021.101028. Epub 2021, Jul 31. PMID:34339732 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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