Crystal Structure of the tRNA 3′ Processing Endoribonuclease tRNase Z from Thermotoga maritima

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, Thermoto...

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Bibliographic Details
Published in:The Journal of biological chemistry 2005-04, Vol.280 (14), p.14138-14144
Main Authors: Ishii, Ryohei, Minagawa, Asako, Takaku, Hiroaki, Takagi, Masamichi, Nashimoto, Masayuki, Yokoyama, Shigeyuki
Format: Article
Language:English
Subjects:
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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Summary: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-Å resolution. The tRNase Z has a four-layer αβ/βα sandwich fold, which is classified as a metallo-β-lactamase fold, and forms a dimer. The active site is located at one edge of the β-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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M500355200