Summary: Glutathione S-transferase, C-terminal domain
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This is the Wikipedia entry entitled "Glutathione S-transferase, C-terminal domain". More...
Glutathione S-transferase, C-terminal domain Edit Wikipedia article
Glutathione S-transferase, C-terminal domain | |||||||||||
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Identifiers | |||||||||||
Symbol | GST_C | ||||||||||
Pfam | PF00043 | ||||||||||
InterPro | IPR004046 | ||||||||||
SCOP2 | 2gst / SCOPe / SUPFAM | ||||||||||
OPM superfamily | 139 | ||||||||||
OPM protein | 1z9h | ||||||||||
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Glutathione S-transferase, C-terminal domain is a structural domain of glutathione S-transferase (GST).
GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants.
The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.
Biological function and classification
In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophilic 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.
Oligomerization
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.
Human proteins containing this domain
EEF1E1; EEF1G; GDAP1; GSTA1; GSTA2; GSTA3; GSTA4; GSTA5; GSTM1; GSTM2; GSTM3; GSTM4; GSTM5; GSTO1; GSTP1; GSTT1; GSTT2; GSTZ1; MARS; PGDS; PTGDS2; PTGES2; VARS;
References
- ^ Armstrong RN (1997). "Structure, catalytic mechanism, and evolution of the glutathione transferases". Chem. Res. Toxicol. 10 (1): 2–18. PMID 9074797.
- ^ 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 (2000). "Identification, characterization, and crystal structure of the Omega class glutathione transferases". J. Biol. Chem. 275 (32): 24798–24806. PMID 10783391.
{{cite journal}}
: line feed character in|author=
at position 34 (help)CS1 maint: multiple names: authors list (link) - ^ Board P, Chelvanayagam G, Dulhunty A, Gage P, Curtis S (2001). "The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator". J. Biol. Chem. 276 (5): 3319–3323. PMID 11035031.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ Eaton DL, Bammler TK (1999). "Concise review of the glutathione S-transferases and their significance to toxicology". Toxicol. Sci. 49 (2): 156–164. PMID 10416260.
- ^ Parker MW, Board PG, Polekhina G, Blackburn AC (2001). "Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity". Biochemistry. 40 (6): 1567–1576. PMID 11327815.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ Vuilleumier S (1997). "Bacterial glutathione S-transferases: what are they good for?". J. Bacteriol. 179 (5): 1431–1441. PMID 9045797.
Further reading
- [1]. Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K; J Mol Biol 1998;281:135-147. PMIDÂ 9680481
- [2]. Plant glutathione transferases. Dixon DP, Lapthorn A, Edwards R; Genome Biol 2002;3:REVIEWS3004. PMIDÂ 11897031
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Glutathione S-transferase, C-terminal domain Provide feedback
This domain is closely related to PF00043.
Internal database links
SCOOP: | Glutaredoxin2_C GST_C GST_C_3 GST_C_4 GST_C_5 GST_C_6 GST_N GST_N_2 GST_N_3 GST_N_4 Tom37 |
Similarity to PfamA using HHSearch: | GST_C Glutaredoxin2_C GST_C_3 GST_C_5 GST_C_6 |
This tab holds annotation information from the InterPro database.
No InterPro data for this Pfam family.
Domain organisation
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Pfam Clan
Alignments
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Seed (135) |
Full (22286) |
Representative proteomes | UniProt (77490) |
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RP15 (2787) |
RP35 (9549) |
RP55 (20064) |
RP75 (34111) |
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HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (135) |
Full (22286) |
Representative proteomes | UniProt (77490) |
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RP15 (2787) |
RP35 (9549) |
RP55 (20064) |
RP75 (34111) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation and family details
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Curation
Seed source: | Jackhmmer:A3PFR8 |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 135 |
Number in full: | 22286 |
Average length of the domain: | 86.8 aa |
Average identity of full alignment: | 19 % |
Average coverage of the sequence by the domain: | 30.14 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 70 | ||||||||||||
Family (HMM) version: | 9 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GST_C_2 domain has been found. There are 257 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.