6LVR

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

6LVR の概要

• エントリーDOI: 10.2210/pdb6lvr/pdb
• 分子名称: Proteinaceous RNase P 1, chloroplastic/mitochondrial, yeast phenylalanine tRNA (3 entities in total)
• 機能のキーワード: protein-only rnase p trna processing trna complex pentatricopeptide repeat convergent evolution, rna binding protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96666.14

構造登録者

Teramoto, T.,Hall, T.M.T. (登録日: 2020-02-04, 公開日: 2020-08-12, 最終更新日: 2023-11-29)

主引用文献

Teramoto, T.,Kaitany, K.J.,Kakuta, Y.,Kimura, M.,Fierke, C.A.,Hall, T.M.T.
Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA.
Nucleic Acids Res., 48:11815-11826, 2020

PubMed Abstract: Pentatricopeptide repeat (PPR) motifs are α-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 Å 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.

PubMed: 32719843
DOI: 10.1093/nar/gkaa627

実験手法

X-RAY DIFFRACTION (2.85 Å)