Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme

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DOIResolve DOI: http://doi.org/10.1128/JB.00650-09
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TypeArticle
Journal titleJournal of Bacteriology
Volume191
Issue24
Pages76147619; # of pages: 6
AbstractThe MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-Å resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedYes
NRC number49586
NPARC number20227905
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Record identifier747e4fa5-52fe-4168-b9de-8ba5ba879024
Record created2012-07-03
Record modified2016-05-09
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