Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of the tRNA 3' processing endoribonuclease tRNase Z from Thermotoga maritima.,Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M, Yokoyama S J Biol Chem. 2005 Apr 8;280(14):14138-44. Epub 2005 Jan 27. PMID:15701599[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M, Yokoyama S. Crystal structure of the tRNA 3' processing endoribonuclease tRNase Z from Thermotoga maritima. J Biol Chem. 2005 Apr 8;280(14):14138-44. Epub 2005 Jan 27. PMID:15701599 doi:10.1074/jbc.M500355200
