In:
Proteins: Structure, Function, and Bioinformatics, Wiley, Vol. 20, No. 3 ( 1994-11), p. 259-263
Kurzfassung:
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 P2 1 2 1 2 1 , with cell dimensions a = 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.
Materialart:
Online-Ressource
ISSN:
0887-3585
,
1097-0134
DOI:
10.1002/prot.340200306
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
1994
ZDB Id:
1475032-6
SSG:
12