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Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme.

Authors :
Rong Shi
Villarroya, Magda
Ruiz-Partida, Rafael
Yunge Li
Proteau, Ariane
Prado, Silvia
Moukadiri, Ismaïl
Benítez-Páez, Alfonso
Lomas, Rodrigo
Wagner, John
Matte, Allan
Velázquez-Campoy, Adrián
Armengod, M.-Eugenia
Cygler, Miroslaw
Source :
Journal of Bacteriology. Dec2009, Vol. 191 Issue 24, p11-11. 1p.
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-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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219193
Volume :
191
Issue :
24
Database :
Academic Search Index
Journal :
Journal of Bacteriology
Publication Type :
Academic Journal
Accession number :
45728763
Full Text :
https://doi.org/10.1128/JB.00650-09