Homology Modeling of Bacillus
subtilis Tryptophanyl-tRNA Synthetase
CHEN Li, JIANG Ge, JIN You-Xin, WANG De-Bao
( State Key Laboratory of Molecular Biology, Institute of Biochemistry and
Cell Biology, Shanghai Institutes of Life Sciences, the Chinese Academy of
Sciences, Shanghai 200031, China )
Abstract
Tryptophanyl-tRNA synthetase (TrpRS) plays a pivotal role in protein synthesis.
However, till now no stereostructural data of Bacillus subtilis TrpRS
were reported. Here, by using the homology modeling using Bacillus
stearothermophilus TrpRS as a template, it is demonstrated that the
synthetase has 16α helices and 5β sheets. The only tryptophan Trp92
is located on the interface of subunits. Also the modeling presents the ligand
binding site, active site and the putative binding of tRNATrp.
Key words tryptophanyl tRNA synthetase； homology modeling； energy optimization； identity amino acid
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