A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal.
A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal.
复制标题
人类 α-谷胱甘肽 S-转移酶的表面突变体 (G82R) 显示出热稳定性降低以及晶体中分子缔合的新模式。
DOI：
10.1002/prot.340200306
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Wang,BC
中科院分区：
文献类型：
--
作者：
Zeng,K;Rose,JP;Chen,HC;Strickland,CL;Tu,CP;Wang,BC
A chimeric enzyme (GST121) of the human α‐glutathione S‐transferases GST1‐1 and GST2‐2, which has improved catalytic efficiency and thermostability from its wild‐type parent proteins, has been crystallized in a space group that is isomorphous with that reported for crystals of GST1‐1. However, a single‐site (G82R) mutant of GST121, which exhibits a significant reduction both in vitro and in vivo in protein thermostability, forms crystals that are not isomorphous with GST1‐1. The mutant protein crystallizes in space group P212121, with cell dimensionsa= 49.5,b= 92.9,c= 115.9 Å, and one dimer per asymmetric unit. Preliminary crystallographic results show that a mutation of the surface residue Gly 82 from a neutral to a charged residue causes new salt bridges to be formed among the GST dimers, suggesting that the G82R mutant might aggregate more readily than does GST121 in solution resulting in a change of its solution properties. © 1994 Wiley‐Liss, Inc.
