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 these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
Rong
R
Shi
Magda
M
Villarroya
Rafael
R
Ruiz-Partida
Yunge
Y
Li
Ariane
A
Proteau
Silvia
S
Prado
Ismaïl
I
Moukadiri
Alfonso
A
Benítez-Páez
Rodrigo
R
Lomas
John
J
Wagner
Allan
A
Matte
Adrián
A
Velázquez-Campoy
M-Eugenia
ME
Armengod
Miroslaw
M
Cygler
D000494:Allosteric Regulation; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012343:RNA, Transfer / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D050505:Mutant Proteins; C108512:glucose-inhibited division protein A, bacteria; D005182:Flavin-Adenine Dinucleotide; D012343:RNA, Transfer; D014357:Trypsin