1WW1

Crystal structure of tRNase Z from Thermotoga maritima

Summary for 1WW1

• Entry DOI: 10.2210/pdb1ww1/pdb
• Descriptor: tRNase Z, ZINC ION (3 entities in total)
• Functional Keywords: metallo-beta-lactamase fold, riken structural genomics/proteomics initiative, rsgi, structural genomics, hydrolase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 65558.03

Authors

Ishii, R.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-12-30, release date: 2005-02-22, Last modification date: 2024-03-13)

Primary citation

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., 280:14138-14144, 2005

PubMed 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.

PubMed: 15701599
DOI: 10.1074/jbc.M500355200

Experimental method

X-RAY DIFFRACTION (2.6 Å)