5ft9 | pdb_00005ft9

Arabidopsis thaliana nuclear protein-only RNase P 2 (PRORP2)

spinqualitylabelsall models 5ft9, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ft9 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Activity: Ribonuclease P, with EC number 3.1.26.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PRRP2_ARATH] Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA). Publication Abstract from PubMed RNase P activity is ubiquitous and involves the 5' maturation of precursor tRNAs. For a long time, it was thought that all RNases P were ribonucleoproteic enzymes. However, the characterization of RNase P in human mitochondria and in plants revealed a novel kind of RNase P composed of protein only, called PRORP for `proteinaceous RNase P'. Whereas in human mitochondria PRORP has two partners that are required for RNase P activity, PRORP proteins are active as single-subunit enzymes in plants. Three paralogues of PRORP are found in Arabidopsis thaliana. PRORP1 is responsible for RNase P in mitochondria and chloroplasts, while PRORP2 and PRORP3 are nuclear enzymes. Here, the purification and crystallization of the Arabidopsis PRORP2 protein are reported. Optimization of the initial crystallization conditions led to crystals that diffracted to 3 A resolution. Crystallization and crystallographic analysis of an Arabidopsis nuclear proteinaceous RNase P.,Pinker F, Giege P, Sauter C Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1372-7. doi:, 10.1107/S2053230X15017033. Epub 2015 Oct 23. PMID:26527263 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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