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Homology Modeling of Bacillus subtilis Tryptophanyl-tRNA Synthetase
1State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes of Life Sciences, the Chinese Academy of Sciences, Shanghai 200031, China. yxjin@sunm.shcnc.ac.cn
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|May 30, 2002
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 16alpha helices and 5beta sheets. The only tryptophan Trp(92) is located on the interface of subunits. Also the modeling presents the ligand binding site, active site and the putative binding of tRNA(Trp).