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

Authors :
Canadian Institutes of Health Research
Ministerio de Ciencia e Innovación (España)
#NODATA#
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
Canadian Institutes of Health Research
Ministerio de Ciencia e Innovación (España)
#NODATA#
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
Publication Year :
2009

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.

Details

Database :
OAIster
Notes :
English
Publication Type :
Electronic Resource
Accession number :
edsoai.on1431960088
Document Type :
Electronic Resource