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tRNA 3′-processing endoribonuclease (tRNase Z) is one of the enzymes involved in the 3′-end processing of precursor tRNAs and is a member of the metallo-β-lactamase superfamily. tRNase Z crystal structures have revealed that the enzyme forms a dimer and has a characteristic domain, named a flexible arm or an exosite, which protrudes from the metallo-β-lactamase core and is involved in tRNA binding. The refined structure of Thermotoga maritima tRNase Z has been determined at 1.97 Å resolution, revealing the structure of the flexible arm and the zinc-bound active site. The structure of the flexible arm of T. maritima tRNase Z is distinct from those of the Bacillus subtilis and Escherichia coli tRNase Zs. A comparison of the three tRNase Z structures revealed differences in the dimer orientation, which may be related to the unique cleavage-site specificity of T. maritima tRNase Z.

Supporting information

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Portable Document Format (PDF) file https://doi.org/10.1107/S1744309107033623/sw5017sup1.pdf
Supplementary material

PDB reference: tRNase Z, 2e7y, r2e7ysf


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