Open AccessStructure of a class II TrmH tRNA‐modifying enzyme from Aquifex aeolicus
Author(s) -
Pleshe Elizabeth,
Truesdell John,
Batey Robert T.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105022980
Subject(s) - aquifex aeolicus , transfer rna , methyltransferase , methylation , bacillus subtilis , biology , enzyme , biochemistry , subfamily , archaea , bacteria , stereochemistry , dna , rna , chemistry , genetics , escherichia coli , gene
Biological RNAs contain a variety of post‐transcriptional modifications that facilitate their efficient function in the cellular environment. One of the two most common forms of modification is methylation of the 2′‐hydroxyl group of the ribose sugar, which is performed by a number of S ‐adenosylmethionine (SAM) dependent methyltransferases. In bacteria, many of these modifications in tRNA and rRNA are carried out by the α/β‐knot superfamily of enzymes, whose SAM‐binding pocket is created by a characteristic deep trefoil knot. TrmH, an enzyme found throughout all three kingdoms of life, modifies the universally conserved guanosine 18 position of tRNA. The crystal structure of TrmH from the thermophilic bacterium Aquifex aeolicus has been determined at 1.85 Å resolution using data collected from a synchrotron‐radiation source. The protein reveals a fold typical of members of the SpoU clan of proteins, a subfamily of the α/β‐knot superfamily, with α‐helical extensions at the N‐ and C‐termini that are likely to be involved in tRNA binding.