InterPro : IPR004045

Name  Glutathione S-transferase, N-terminal Short Name  Glutathione_S-Trfase_N
Type  Domain Description  In eukaryotes, glutathione S-transferases (GSTs) participate in thedetoxification of reactive electrophillic compounds by catalysing theirconjugation to glutathione. The GST domain is also found in S-crystallins from squid, and proteins with no known GST activity, such as eukaryotic elongation factors 1-gamma and the HSP26 family of stress-related proteins, which include auxin-regulated proteins in plants and stringent starvation proteins in Escherichia coli. The major lens polypeptide of Cephalopoda is also a GST [, , , ].Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs. Some regulatory proteins, like the stringent starvation proteins, also belong to the GST family [, ]. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.Soluble GSTs activate glutathione (GSH) to GS-. In many GSTs, this is accomplished by a Tyr at H-bonding distance from the sulphur of GSH. These enzymes catalyse nucleophilic attack by reduced glutathione (GSH) on nonpolar compounds that contain an electrophillic carbon, nitrogen, or sulphur atom [].Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold, with each monomer composed of two distinct domains []. The N-terminal domain forms a thioredoxin-like fold that binds the glutathione moiety, while the C-terminal domain contains several hydrophobic alpha-helices that specifically bind hydrophobic substrates.This entry represents the N-terminal domain of GST.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

8 Found In

Id Name Short Name Type
IPR003081 Glutathione S-transferase, Mu class GST_mu Family
IPR005955 Maleylacetoacetate isomerase Mal_ac_isom Family
IPR011901 Glutaredoxin, GrxB GRXB Family
IPR005442 Glutathione S-transferase, omega-class GST_omega Family
IPR003080 Glutathione S-transferase, alpha class GST_alpha Family
IPR003082 Glutathione S-transferase, Pi class GST_pi Family
IPR003083 S-crystallin S-crystallin Family
IPR017298 Transcriptional regulator Ure2 Ure2 Family

1 Parent Features

Id Name Short Name Type
IPR012336 Thioredoxin-like fold Thioredoxin-like_fold Domain

8 Publications

First Author Title Year Journal Volume Pages
Armstrong RN Structure, catalytic mechanism, and evolution of the glutathione transferases. 1997 Chem Res Toxicol 10 2-18
Board PG Identification, characterization, and crystal structure of the Omega class glutathione transferases. 2000 J Biol Chem 275 24798-806
Dulhunty A The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. 2001 J Biol Chem 276 3319-23
Eaton DL Concise review of the glutathione S-transferases and their significance to toxicology. 1999 Toxicol Sci 49 156-64
Polekhina G Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. 2001 Biochemistry 40 1567-76
Vuilleumier S Bacterial glutathione S-transferases: what are they good for? 1997 J Bacteriol 179 1431-41
Le Trong I 1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site. 2002 Proteins 48 618-27
Mannervik B Nomenclature for mammalian soluble glutathione transferases. 2005 Methods Enzymol 401 1-8



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)