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5gst

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REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE

Structural highlights

5gst is a 2 chain structure with sequence from Rattus rattus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GSTM1_RAT Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase.,Ji X, Armstrong RN, Gilliland GL Biochemistry. 1993 Dec 7;32(48):12949-54. PMID:8241147^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ji X, Armstrong RN, Gilliland GL. Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase. Biochemistry. 1993 Dec 7;32(48):12949-54. PMID:8241147