PMID:15701599

Citation	Ishii, R, Minagawa, A, Takaku, H, Takagi, M, Nashimoto, M and Yokoyama, S (2005) Crystal structure of the tRNA 3' processing endoribonuclease tRNase Z from Thermotoga maritima. J. Biol. Chem. 280:14138-44
Abstract	The maturation of the tRNA 3' end is catalyzed by a tRNA 3' processing endoribonuclease named tRNase Z (RNase Z or 3'-tRNase) in eukaryotes, Archaea, and some bacteria. The tRNase Z generally cuts the 3' extra sequence from the precursor tRNA after the discriminator nucleotide. In contrast, Thermotoga maritima tRNase Z cleaves the precursor tRNA precisely after the CCA sequence. In this study, we determined the crystal structure of T. maritima tRNase Z at 2.6-A resolution. The tRNase Z has a four-layer alphabeta/betaalpha sandwich fold, which is classified as a metallo-beta-lactamase fold, and forms a dimer. The active site is located at one edge of the beta-sandwich and is composed of conserved motifs. Based on the structure, we constructed a docking model with the tRNAs that suggests how tRNase Z may recognize the substrate tRNAs.
Links	PubMed Online version:10.1074/jbc.M500355200
Keywords	Amino Acid Sequence; Animals; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Crystallography, X-Ray; Endoribonucleases/chemistry; Endoribonucleases/metabolism; Humans; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Structure, Tertiary; RNA Processing, Post-Transcriptional; RNA, Transfer/chemistry; RNA, Transfer/metabolism; Sequence Alignment; Thermotoga maritima/enzymology; Thermotoga maritima/genetics
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