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Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain

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JournalJournal of Molecular Biology
DatePublished - 10 Feb 2006
Issue number1
Volume356
Number of pages14
Pages (from-to)97-110
Original languageEnglish

Abstract

ThiI is an enzyme responsible for the formation of the modified base (SU)-U-4 (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This base acts as a sensitive trigger for the response mechanism to UV exposure, providing protection against its damaging effects. We present the crystal structure of Bacillus anthracis ThiI in complex with AMP, revealing an extended tripartite architecture in which an N-terminal ferredoxin-like domain (NFLD) connects the C-terminal catalytic PP-loop pyrophosphatase domain with a THUMP domain, an ancient predicted RNA-binding domain that is widespread in all kingdoms of life. We describe the structure of the THUMP domain, which appears to be unrelated to RNA-binding domains of known structure. Mapping the conserved residues of NFLD and the THUMP domain onto the ThiI structure suggests that these domains jointly form the tRNA-binding surface. The inaccessibility of U8 in the canonical L-shaped form of tRNA, and the existence of a glycine-rich linker joining the catalytic and RNA-binding moieties of ThiI suggest that structural changes may occur in both molecules upon binding. (c) 2005 Elsevier Ltd. All rights reserved.

    Research areas

  • ThiI, THUMP domain, RNA binding, tRNA modification, X-ray crystallography, ESCHERICHIA-COLI, GROWTH DELAY, 4-THIOURIDINE BIOSYNTHESIS, SALMONELLA-TYPHIMURIUM, MODIFIED NUCLEOSIDES, POLYKETIDE SYNTHASE, MOLECULAR-GRAPHICS, PROTEIN STRUCTURES, SEQUENCE, GENE

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