1ww1
From Proteopedia
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| , resolution 2.60Å | |||||||
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| Ligands: | |||||||
| Activity: | Ribonuclease Z, with EC number 3.1.26.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of tRNase Z from Thermotoga maritima
Overview
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.
About this Structure
1WW1 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 00:41:43 2008
