Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution

Mycobacterium tuberculosis glutamyl-tRNA synthetase (Mt-GluRS), encoded by Rv2992c, was overproduced in Escherichia coli cells, and purified to homogeneity. It was found to be similar to the other well-characterized GluRS, especially the E. coli enzyme, with respect to the requirement for bound tRNA...

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Veröffentlicht in:	The FEBS journal 2009-03, Vol.276 (5), p.1398-1417
Hauptverfasser:	Paravisi, Stefano, Fumagalli, Gianluca, Riva, Milena, Morandi, Paola, Morosi, Rachele, Konarev, Peter V, Petoukhov, Maxim V, Bernier, Stéphane, Chênevert, Robert, Svergun, Dmitri I, Curti, Bruno, Vanoni, Maria A
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biochemistry Cellular biology E coli Escherichia coli - genetics Escherichia coli - metabolism Glutamate-tRNA Ligase - chemistry Glutamate-tRNA Ligase - metabolism glutamyl-tRNA reductase glutamyl-tRNA synthetase Kinetics Molecular Sequence Data Mycobacterium tuberculosis Mycobacterium tuberculosis - enzymology protein synthesis Ribonucleic acid RNA RNA, Transfer - metabolism RNA, Transfer, Amino Acyl - chemistry RNA, Transfer, Amino Acyl - metabolism Solutions tetrapyrrole synthesis Tuberculosis
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