Glutathione S-transferase, C-terminal domain

Glutathione S-transferase, C-terminal domain is a structural domain of glutathione S-transferase (GST).

GST conjugates reduced glutathione to a variety of targets includingS-crystallin from squid, the eukaryotic elongation factor1-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-terminaldomain. 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 GSTcite journal |author=Armstrong RN |title=Structure, catalytic mechanism, and evolution of the glutathione transferases |journal=Chem. Res. Toxicol. |volume=10 |issue=1 |pages=2–18 |year=1997 |pmid=9074797 |doi=10.1021/tx960072x] cite journal |author=Board PG, Coggan M, ChelvanayagamG, 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 |title=Identification, characterization, and crystal structure of the Omega class glutathione transferases |journal=J. Biol. Chem. |volume=275 |issue=32 |pages=24798–24806 |year=2000 |pmid=10783391 |doi=10.1074/jbc.M001706200] cite journal |author=Board P, Chelvanayagam G, Dulhunty A, Gage P, Curtis S |title=The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator |journal=J. Biol. Chem. |volume=276 |issue=5 |pages=3319–3323 |year=2001 |pmid=11035031 |doi=10.1074/jbc.M007874200] cite journal |author=Eaton DL, Bammler TK |title=Concise review of the glutathione S-transferases and their significance to toxicology |journal=Toxicol. Sci. |volume=49 |issue=2 |pages=156–164 |year=1999 |pmid=10416260 |doi=10.1093/toxsci/49.2.156] .

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 familycite journal |author=Parker MW, Board PG, Polekhina G, Blackburn AC |title=Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity |journal=Biochemistry |volume=40 |issue=6 |pages=1567–1576 |year=2001 |pmid=11327815 |doi=10.1021/bi002249z] cite journal |author=Vuilleumier S |title=Bacterial glutathione S-transferases: what are they good for? |journal=J. Bacteriol. |volume=179 |issue=5 |pages=1431–1441 |year=1997 |pmid=9045797] . 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

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. PMID|9680481
* [2] . Plant glutathione transferases. Dixon DP, Lapthorn A, Edwards R; Genome Biol 2002;3:REVIEWS3004. PMID|11897031

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