1ags
|
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
OverviewOverview
A chimeric enzyme (GST121) of the human alpha-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 A, 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.
About this StructureAbout this Structure
1AGS is a Single protein structure of sequence from Synthetic construct with GTX as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
ReferenceReference
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., Zeng K, Rose JP, Chen HC, Strickland CL, Tu CP, Wang BC, Proteins. 1994 Nov;20(3):259-63. PMID:7892174
Page seeded by OCA on Mon Nov 12 15:58:28 2007