Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Allosteric Regulation
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Crystallography, X-Ray
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Escherichia coli / enzymology*
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Flavin-Adenine Dinucleotide / metabolism
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Models, Molecular
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Mutagenesis, Site-Directed
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Mutant Proteins / genetics
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Mutant Proteins / metabolism
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Protein Binding
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Protein Structure, Tertiary
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RNA, Transfer / metabolism*
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Trypsin / metabolism
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Mutant Proteins
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glucose-inhibited division protein A, bacteria
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Flavin-Adenine Dinucleotide
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RNA, Transfer
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Trypsin