6lvr

Crystal structure of the PPR domain of Arabidopsis thaliana protein-only RNase P 1 (PRORP1) in complex with tRNA

spinqualitylabelsall models 6lvr, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lvr is a 4 chain structure with sequence from Arabidopsis thaliana and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.85Å Ligands: 1MA, 2MG, 5MC, 5MU, 7MG, H2U, M2G, OMC, OMG, PSU, YYG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRRP1_ARATH Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Preferentially cleaves at the unusual cleavage site, but also able to cleave at the classical cleavage site. Also involved in the maturation of mRNAs in mitochondria. Publication Abstract from PubMed Pentatricopeptide repeat (PPR) motifs are alpha-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana is an endoribonuclease that uses its PPR domain to recognize precursor tRNAs (pre-tRNAs) as it catalyzes removal of the 5'-leader sequence from pre-tRNAs with its NYN metallonuclease domain. To gain insight into the mechanism by which PRORP1 recognizes tRNA, we determined a crystal structure of the PPR domain in complex with yeast tRNAPhe at 2.85 A resolution. The PPR domain of PRORP1 bound to the structurally conserved elbow of tRNA and recognized conserved structural features of tRNAs using mechanisms that are different from the established single-stranded RNA recognition mode of PPR motifs. The PRORP1 PPR domain-tRNAPhe structure revealed a conformational change of the PPR domain upon tRNA binding and moreover demonstrated the need for pronounced overall flexibility in the PRORP1 enzyme conformation for substrate recognition and catalysis. The PRORP1 PPR motifs have evolved strategies for protein-tRNA interaction analogous to tRNA recognition by the RNA component of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solution for tRNA substrate recognition. Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA.,Teramoto T, Kaitany KJ, Kakuta Y, Kimura M, Fierke CA, Hall TMT Nucleic Acids Res. 2020 Dec 2;48(21):11815-11826. doi: 10.1093/nar/gkaa627. PMID:32719843 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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