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

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...

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Detalles Bibliográficos
Autores: Shi, Rong, Villarroya, Magda, Ruiz-Partida, Rafael, Li, Yunge, Proteau, Ariane, Prado, Silvia, Moukadiri, Ismaïl, Benítez-Páez, Alfonso, Lomas, Rodrigo, Wagner, John, Matte, Allan, Velázquez-Campoy, Adrián, Armengod, M-Eugenia, Cygler, Miroslaw
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2009
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/344983
Acceso en línea:http://hdl.handle.net/10261/344983
https://api.elsevier.com/content/abstract/scopus_id/72449211907
Access Level:acceso abierto
Palabra clave:Escherichia coli
MnmG
tRNA modification
Descripción
Sumario: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.

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