| DOI | Resolve DOI: https://doi.org/10.1128/JB.00650-09 |
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| Author | Search for: Shi, Rong; Search for: Villarroya, Magda; Search for: Ruiz-Partida, Rafael; Search for: Li, Yunge1; Search for: Proteau, Ariane; Search for: Prado, Silvia; Search for: Moukadiri, Ismail; Search for: Benitez-Paez, Alfonso; Search for: Lomas, Rodrigo; Search for: Wagner, John1; Search for: Matte, Allan1; Search for: Velazquez-Campoy, Adrian; Search for: Armengod, M.-Eugenia; Search for: Cygler, Miroslaw1 |
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| Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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| Format | Text, Article |
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| Abstract | The 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. |
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| Publication date | 2009-10-02 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | NRCC 49586 |
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| NPARC number | 20227905 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 747e4fa5-52fe-4168-b9de-8ba5ba879024 |
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| Record created | 2012-07-03 |
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| Record modified | 2020-04-16 |
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