Structures of thermolabile mutants of human glutathione transferase P1-1.
Structures of thermolabile mutants of human glutathione transferase P1-1.
复制标题
人谷胱甘肽转移酶 P1-1 不耐热突变体的结构。
DOI：
--
复制
发表时间：
2000
影响因子：
5.6
通讯作者：
A. Aceto
中科院分区：
文献类型：
--
作者：
J. Rossjohn;W. McKinstry;A. Oakley;M. Parker;G. Stenberg;B. Mannervik;B. Dragani;R. Cocco;A. Aceto
An N-capping box motif (Ser/Thr-Xaa-Xaa-Asp) is strictly conserved at the beginning of helix alpha6 in the core of virtually all glutathione transferases (GST) and GST-related proteins. It has been demonstrated that this local motif is important in determining the alpha-helical propensity of the isolated alpha6-peptide and plays a crucial role in the folding and stability of GSTs. Its removal by site-directed mutagenesis generated temperature-sensitive folding mutants unable to refold at physiological temperature (37 degrees C). In the present work, variants of human GSTP1-1 (S150A and D153A), in which the capping residues have been substituted by alanine, have been generated and purified for structural analysis. Thus, for the first time, temperature-sensitive folding mutants of an enzyme, expressed at a permissive temperature, have been crystallized and their three-dimensional structures determined by X-ray crystallography. The crystal structures of human pi class GST temperature-sensitive mutants provide a basis for understanding the structural origin of the dramatic effects observed on the overall stability of the enzyme at higher temperatures upon single substitution of a capping residue.
影响因子：
56.9
作者：
PRESTA, LG;ROSE, GD
通讯作者：
ROSE, GD
孤立的α螺旋中的加帽相互作用：位置依赖性取代效应和丝氨酸加帽的肽螺旋的结构。
影响因子：
2.9
作者：
Lyu,PC;Wemmer,DE;Zhou,HX;Pinker,RJ;Kallenbach,NR
通讯作者：
Kallenbach,NR
DOI：
10.1073/pnas.90.3.838
发表时间：
1993-02-01
影响因子：
11.1
作者：
FOROOD, B;FELICIANO, EJ;NAMBIAR, KP
通讯作者：
NAMBIAR, KP