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InterPro: IPR004046 Glutathione S-transferase, C-terminal

Protein matches Help

UniProtKB

Matches:

8895 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004046 GST_C

Secondary

IPR000521

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00043	GST_C	8895
Signatures in BioMart

InterPro Relationships Help

Parent

IPR017933 Glutathione S-transferase/chloride channel, C-terminal

Found in

IPR003080 Glutathione S-transferase, alpha class
IPR003081 Glutathione S-transferase, Mu class
IPR003082 Glutathione S-transferase, Pi class
IPR005442 Glutathione S-transferase, omega-class
IPR005955 Maleylacetoacetate isomerase
IPR016639 Glutathione S-transferase, predicted
IPR017298 Prion URE2

Contains

IPR003083 S-crystallin/Sigma class glutathione-S-transferase

InterPro annotation

Entry Details in BioMart

Abstract

In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophillic compounds by catalysing their conjugation 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 cephalopods is also a GST [1, 2, 3, 4].

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 [5, 6]. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.

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. Each monomer is composed of a distinct N-terminal sub-domain, which adopts the thioredoxin fold, and a C-terminal all-helical sub-domain. This entry is the C-terminal domain.

Structural links Help

PDB - click here

SCOP: a.45.1.1

CATH: 1.20.1050.10 , 3.40.30.10

Database links Help

PANDIT: PF00043

Blocks: IPB004046

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004046

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O15217 Glutathione S-transferase A4

P10648 Glutathione S-transferase A2

P20432 Glutathione S-transferase 1-1

P23202 Protein URE2

Q09596 Probable glutathione S-transferase 5

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010987	Glutathione S-transferase, C-terminal-like
IPR003080	Glutathione S-transferase, alpha class
IPR012336	Thioredoxin-like fold
IPR004046	Glutathione S-transferase, C-terminal
IPR004045	Glutathione S-transferase, N-terminal
IPR017933	Glutathione S-transferase/chloride channel, C-terminal
IPR012335	Thioredoxin fold
IPR017298	Prion URE2
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Armstrong RN. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10 2-18 1997 [PubMed: 9074797] http://dx.doi.org/10.1021/tx960072x
2.	Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J. Identification, characterization, and crystal structure of the Omega class glutathione transferases. J. Biol. Chem. 275 24798-806 2000 [PubMed: 10783391] http://dx.doi.org/10.1074/jbc.M001706200
3.	Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P. The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. J. Biol. Chem. 276 3319-23 2001 [PubMed: 11035031] http://dx.doi.org/10.1074/jbc.M007874200
4.	Eaton DL, Bammler TK. Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol. Sci. 49 156-64 1999 [PubMed: 10416260] http://dx.doi.org/10.1093/toxsci/49.2.156
5.	Polekhina G, Board PG, Blackburn AC, Parker MW. Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry 40 1567-76 2001 [PubMed: 11327815] http://dx.doi.org/10.1021/bi002249z
6.	Vuilleumier S. Bacterial glutathione S-transferases: what are they good for? J. Bacteriol. 179 1431-41 1997 [PubMed: 9045797] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9045797

Additional Reading Open in usermanual
	Hohwy M, Spadola L, Lundquist B, Hawtin P, Dahmen J, Groth-Clausen I, Nilsson E, Persdotter S, von Wachenfeldt K, Folmer RH, Edman K. Novel prostaglandin D synthase inhibitors generated by fragment-based drug design. J. Med. Chem. 51 2008 2178-86 [PubMed: 18341273] http://dx.doi.org/10.1021/jm701509k
	Dixon DP, Lapthorn A, Edwards R. Plant glutathione transferases. Genome Biol. 3 2002 REVIEWS3004 [PubMed: 11897031] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=11897031
	Hegazy UM, Tars K, Hellman U, Mannervik B. Modulating catalytic activity by unnatural amino acid residues in a GSH-binding loop of GST P1-1. J. Mol. Biol. 376 2008 811-26 [PubMed: 18177897] http://dx.doi.org/10.1016/j.jmb.2007.12.013
	Parker LJ, Ciccone S, Italiano LC, Primavera A, Oakley AJ, Morton CJ, Hancock NC, Bello ML, Parker MW. The anti-cancer drug chlorambucil as a substrate for the human polymorphic enzyme glutathione transferase P1-1: kinetic properties and crystallographic characterisation of allelic variants. J. Mol. Biol. 380 2008 131-44 [PubMed: 18511072] http://dx.doi.org/10.1016/j.jmb.2008.04.066
	Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C. Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site. Proteins 71 2008 16-23 [PubMed: 18076047] http://dx.doi.org/10.1002/prot.21835
	Perbandt M, Hoppner J, Burmeister C, Luersen K, Betzel C, Liebau E. Structure of the extracellular glutathione S-transferase OvGST1 from the human pathogenic parasite Onchocerca volvulus. J. Mol. Biol. 377 2008 501-11 [PubMed: 18258257] http://dx.doi.org/10.1016/j.jmb.2008.01.029
	Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K. Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. J. Mol. Biol. 281 1998 135-47 [PubMed: 9680481] http://dx.doi.org/10.1006/jmbi.1998.1927

InterPro 23.1