Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.

@article{Kawasaki2002AlternateCO,
  title={Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.},
  author={Kosei Kawasaki and Hidemasa Kondo and Mamoru Suzuki and Satoru Ohgiya and Sakae Tsuda},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2002},
  volume={58 Pt 7},
  pages={
          1168-74
        }
}
Bacillus subtilis extracellular lipase (BsL) has an exceptionally low molecular weight (19.4 kDa) for a member of the lipase family. A crystallographic study was performed on BsL in order to design and produce mutant BsL that will be more suitable for industrial uses based on analysis of the three-dimensional structure. Recently, the crystal structure of BsL has been determined at 1.5 A resolution [van Pouderoyen et al. (2001). J. Mol. Biol. 309, 215-226]. In the present study, a new crystal… CONTINUE READING

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