[A model of three-dimensional structure of Mycobacterium tuberculosis tyrosyl-tRNA synthetase].
The search of new effective antibacterial drugs against infectious agents also lately include inhibitors of some aminoacyl-tRNA synthetases. In this regard, tyrosyl-tRNA synthetase from M. tuberculosis (MtTyrRS) is one of especially attractive target due to its key role in cell metabolism and significant differences between spatial structures of eubacterial and human TyrRSs. In this article the theoretic homology modeling of spatial structure of catalytic module of MtTyrRS (region Met1-Ser321) has been carried out based on experimentally determined structures of homologous TyrRSs from other eubacteria, and the comparison of the structures of their active sites was performed. Most of MtTyrRS catalytic site residues, particularly those, which form special hydrogen bonds with low-molecular-weight ligands (Tyr36, Asp80, Tyrl71, Asp178, Gly194 and Asp196) as well catalytic residues Lys231 and Lys234 from KFGK motif of interdomain loop and Arg87, are conservative in evolution.
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D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D003198:Computer Simulation; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000187:drug effects / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D014448:Tyrosine-tRNA Ligase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification
D014448:Tyrosine-tRNA Ligase