Detalle de: Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme
| Title | Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme |
| 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. |
| Apa Reference | Shi, R., Villarroya, M., Ruiz-Partida, R., Li, Y., Proteau, A., Prado, S., Moukadiri, I., Benítez-Páez, A., Lomas, R., Wagner, J., Matte, A., Velázquez-Campoy, A., Armengod, M.-E., & Cygler, M. (2009). Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme. Journal of Bacteriology, 191(24), 7614–7619. 10.1128/jb.00650-09 |
| Doi | 10.1128/jb.00650-09 |
| Publication Date | 15 Dec 2009 |
| Publication Type | Article |
| Researcher | Alfonso Benítez Páez |
| Ontology | Model organisms, Structural bioinformatics, Experimental structure determination, Molecular flexibility, Conservation Analysis, Structure-function relationship |
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