Large conformational changes in the catalytic cycle of glutathione synthase

被引:32
作者
Gogos, A
Shapiro, L
机构
[1] Columbia Univ Coll Phys & Surg, Dept Biochem & Mol Biophys, New York, NY 10032 USA
[2] Columbia Univ Coll Phys & Surg, Dept Ophthalmol, New York, NY 10032 USA
[3] Columbia Univ Coll Phys & Surg, Naomi Berrie Diabet Ctr, New York, NY 10032 USA
关键词
glutathione synthase; ATP-grasp superfamily; substrate complex; product complex; crystal structure; conformational change;
D O I
10.1016/S0969-2126(02)00906-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Glutathione synthase catalyzes the final ATP-dependent step in glutathione biosynthesis, the formation of glutathione from gamma-glutamylcysteine and glycine. We have determined structures of yeast glutathione synthase in two forms: unbound (2.3 Angstrom resolution) and bound to its substrate gamma-glutamylcysteine, the ATP analog AMP-PNP, and two magnesium ions (1.8 Angstrom resolution). These structures reveal that upon substrate binding, large domain motions convert the enzyme from an open unliganded form to a closed conformation in which protein domains completely surround the substrate in the active site.
引用
收藏
页码:1669 / 1676
页数:8
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