1EOH

GLUTATHIONE TRANSFERASE P1-1

Summary for 1EOH

• Entry DOI: 10.2210/pdb1eoh/pdb
• Related: 1EOG 9gss
• Descriptor: GLUTATHIONE S-TRANSFERASE (2 entities in total)
• Functional Keywords: glutathione transferase, helix capping mutant (d152a), transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 8
• Total formula weight: 185620.49

Authors

Rossjohn, J.,McKinstry, W.J.,Oakley, A.J.,Parker, M.W.,Stenberg, G.,Mannervik, B.,Dragani, B.,Cocco, R.,Aceto, A. (deposition date: 2000-03-22, release date: 2000-10-18, Last modification date: 2024-02-07)

Primary citation

Rossjohn, J.,McKinstry, W.J.,Oakley, A.J.,Parker, M.W.,Stenberg, G.,Mannervik, B.,Dragani, B.,Cocco, R.,Aceto, A.
Structures of thermolabile mutants of human glutathione transferase P1-1.
J.Mol.Biol., 302:295-302, 2000

PubMed Abstract: 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.

PubMed: 10970734
DOI: 10.1006/jmbi.2000.4054

Experimental method

X-RAY DIFFRACTION (2.5 Å)