Glutathione S-transferase, C-terminal domain

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Glutathione S-transferase, C-terminal domain
Identifiers
Symbol GST_C
Pfam PF00043
InterPro IPR004046
SCOP 2gst
OPM family 139
OPM protein 1z9h
Available PDB structures:

1gnwA:111-206 1bx9A:111-206 1aw9 :107-202 1byeB:110-201 1axdA:110-201 1pn9B:104-190 1jlvB:111-185 1r5aA:126-192 1n2aA:100-189 1a0fB:100-189 2pmtB:100-189 1pmt :100-189 1f2eD:100-189 1nhyA:107-199 2cz3A:105-197 2cz2A:105-197 1fw1A:153-197 1e6bA:111-203 1oe7A:102-196 1oe8A:102-196 1u3iA:102-196 1k0dC:223-345 1hqoA:223-345 1k0bC:223-345 1k0cA:223-345 1g6yB:223-345 1k0aA:223-345 1g6wC:223-345 1jzrD:223-345 2ljrA:128-201 1ljrB:128-201 2c3nD:111-200 2c3tD:111-200 2c3qD:111-200 1v2aC:103-188 1z9hB:276-370 1eemA:114-210 1oyjC:106-205 1gwcB:122-203 1gumE:100-192 1xwgA:99-192 1pl2B:99-192 1pkwB:99-192 1pkzB:99-192 1usbA:99-192 1guhA:99-192 1pl1B:99-192 1gsdA:99-192 1gsfA:99-192 1k3lB:99-192 1gseA:99-192 1k3oB:99-192 1ydkA:99-192 1k3yB:99-192 1tdiA:99-192 1ml6A:99-192 1f3bA:99-192 1f3aB:99-192 1ev9A:99-192 1ev4A:99-192 1vf3A:99-192 1vf2B:99-192 1vf1A:99-192 1vf4A:99-192 1gukA:99-192 1b48B:99-192 1oktA:134-197 1zl9B:109-193 1tw9H:143-190 1yq1B:128-194 1iyhC:131-185 1v40C:131-185 1iyiA:131-185 1pd22:131-185 1b4pA:104-192 6gswA:104-192 6gsuA:104-192 6gsvB:104-192 6gstA:104-192 4gstA:104-192 6gsxA:104-192 6gsyA:104-192 1mtcA:104-192 3fygB:104-192 5gstA:104-192 5fwgB:104-192 3gstB:104-192 2gstA:104-192 4gtuE:104-192 1xw6B:104-192 1yj6C:104-192 1xwkA:104-192 1gtuC:104-192 3gtuC:104-192 1xw5B:104-192 1hnbB:104-192 2ab6B:104-192 2c4jB:104-192 1hncA:104-192 1hna :104-192 2gtuA:104-192 1ykcB:104-192 1c72A:104-192 1gsuA:104-192 1fhe :99-187 2fheB:98-186 1gtb :99-187 1u88A:99-187 1m9bA:99-187 1gta :99-187 1ua5A:99-187 1m9aA:99-187 1m99A:99-187 1y6eB:99-187 1bg5 :99-187 1u87A:99-187 1b8xA:99-187 1gne :99-187 1gtiE:97-188 1gsyB:97-188 1glpA:97-188 1glqA:97-188 2glrB:97-188 1bayB:97-188 1lx2A:97-188 1md3B:97-188 18gsA:97-188 19gsA:97-188 7gssB:97-188 1aqwA:97-188 20gsA:97-188 1eogB:97-188 1md4B:97-188 9gssA:97-188 2pgtB:97-188 8gssC:97-188 1aqvA:97-188 1eohE:97-188 5gssA:97-188 1pgtA:97-188 22gsB:97-188 21gsA:97-188 1zgnB:97-188 6gssA:97-188 1px7B:97-188 14gsB:97-188 3pgtB:97-188 1aqxB:97-188 1px6A:97-188 17gsB:97-188 16gsB:97-188 1kbnA:97-188 4gssA:97-188 3gssB:97-188 11gsA:97-188 2gssB:97-188 4pgtB:97-188 2gsrA:94-185 1tu8B:94-186 1tu7B:94-186 1m0uA:141-235 2gsq :95-189 1gsq :95-189

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.

Contents

[edit] 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.

[edit] 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.

[edit] 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;

[edit] References

  1. ^ Armstrong RN (1997). "Structure, catalytic mechanism, and evolution of the glutathione transferases". Chem. Res. Toxicol. 10 (1): 2–18. doi:10.1021/tx960072x. PMID 9074797. 
  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 (2000). "Identification, characterization, and crystal structure of the Omega class glutathione transferases". J. Biol. Chem. 275 (32): 24798–24806. doi:10.1074/jbc.M001706200. PMID 10783391. 
  3. ^ 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. doi:10.1074/jbc.M007874200. PMID 11035031. 
  4. ^ Eaton DL, Bammler TK (1999). "Concise review of the glutathione S-transferases and their significance to toxicology". Toxicol. Sci. 49 (2): 156–164. doi:10.1093/toxsci/49.2.156. PMID 10416260. 
  5. ^ 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. doi:10.1021/bi002249z. PMID 11327815. 
  6. ^ Vuilleumier S (1997). "Bacterial glutathione S-transferases: what are they good for?". J. Bacteriol. 179 (5): 1431–1441. PMID 9045797. 

[edit] 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. PubMed
  • [2]. Plant glutathione transferases. Dixon DP, Lapthorn A, Edwards R; Genome Biol 2002;3:REVIEWS3004. PubMed
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