The structure of a reduced mutant T4 glutaredoxin

FEBS Letters

Eklund, Hans¹  Nordlund, Pär¹  Ingelman, Margareta¹ 

[1]Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Center, Box 590, S-751 24 Uppsala, Sweden

关键词: Glutaredoxin;    Redox-active thiols;    Disulfide reduction;    Crystallography;    Mutant protein;   

DOI  :  10.1016/0014-5793(95)00806-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown