Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.
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ABSTRACT:
SUBMITTER: Shi R
PROVIDER: S-EPMC2786596 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
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Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.
Shi Rong R Villarroya Magda M Ruiz-Partida Rafael R Li Yunge Y Proteau Ariane A Prado Silvia S Moukadiri Ismaïl I Benítez-Páez Alfonso A Lomas Rodrigo R Wagner John J Matte Allan A Velázquez-Campoy Adrián A Armengod M-Eugenia ME Cygler Miroslaw M
Journal of bacteriology 20091002 24
The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A 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. ...[more]
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