5GST

REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE

Summary for 5GST

• Entry DOI: 10.2210/pdb5gst/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, SULFATE ION, GLUTATHIONE S-(2,4 DINITROBENZENE), ... (4 entities in total)
• Functional Keywords: glutathione transferase, transferase
• Biological source: Rattus rattus (black rat)
• Cellular location: Cytoplasm: P04905
• Total number of polymer chains: 2
• Total formula weight: 52680.48

Authors

Ji, X.,Armstrong, R.N.,Gilliland, G.L. (deposition date: 1993-07-20, release date: 1993-10-31, Last modification date: 2023-08-30)

Primary citation

Ji, X.,Armstrong, R.N.,Gilliland, G.L.
Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase.
Biochemistry, 32:12949-12954, 1993

PubMed Abstract: The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.

PubMed: 8241147
DOI: 10.1021/bi00211a001

Experimental method

X-RAY DIFFRACTION (2 Å)