Ingelman M, Nordlund P, Eklund H
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
FEBS Lett. 1995 Aug 21;370(3):209-11. doi: 10.1016/0014-5793(95)00806-k.
The mutant T4 glutaredoxin where the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, crystallizes in a form where the active site disulfide is accessible to reagents. Treatment of the crystals with dithiotreitol causes very subtle changes in the overall glutaredoxin structure. The main differences are seen around the active site where the sulfurs of Cys14 and Cys17 move apart slightly.
活性位点残基Val15和Tyr16分别被Gly和Pro取代的突变型T4谷氧还蛋白，以活性位点二硫键可被试剂接触到的形式结晶。用二硫苏糖醇处理晶体，会使谷氧还蛋白的整体结构发生非常细微的变化。主要差异出现在活性位点周围，其中Cys14和Cys17的硫原子会略微分开。
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