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• W2047337487 abstract "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-beta-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-beta-lactamase core and is involved in tRNA binding. The refined structure of Thermotoga maritima tRNase Z has been determined at 1.97 A 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." @default.
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• W2047337487 date "2007-07-21" @default.
• W2047337487 modified "2023-10-03" @default.
• W2047337487 title "The structure of the flexible arm of<i>Thermotoga maritima</i>tRNase Z differs from those of homologous enzymes" @default.
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• W2047337487 doi "https://doi.org/10.1107/s1744309107033623" @default.
• W2047337487 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2335171" @default.
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