Article
Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.
The Journal of biological chemistry - 26 Jul 2002
Almog Orna, Gallagher D T, Ladner Jane E, Strausberg Susan, Alexander Patrick, Bryan Philip, Gilliland Gary L
Abstract excerpt
The crystal structures of two thermally stabilized subtilisin BPN' variants, S63 and S88, are reported here at 1.8 and 1.9 A resolution, respectively. The micromolar affinity calcium binding site (site A) has been deleted (Delta75-83) in these variants, enabling the activity and thermostability measurements in chelating conditions. Each of the variants includes mutations known previously to increase the...
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