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

Summary for 1AGS

• Entry DOI: 10.2210/pdb1ags/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE ALPHA, S-HEXYLGLUTATHIONE (2 entities in total)
• Functional Keywords: transferase (glutathione)
• Biological source: synthetic construct
• Cellular location: Cytoplasm: P09210
• Total number of polymer chains: 2
• Total formula weight: 52159.02

Authors

Zeng, K.,Rose, J.P.,Wang, B.C. (deposition date: 1995-01-23, release date: 1995-07-10, Last modification date: 2024-02-07)

Primary citation

Zeng, K.,Rose, J.P.,Chen, H.C.,Strickland, C.L.,Tu, C.P.,Wang, B.C.
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.
Proteins, 20:259-263, 1994

PubMed Abstract: 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.

PubMed: 7892174
DOI: 10.1002/prot.340200306

Experimental method

X-RAY DIFFRACTION (2.5 Å)