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.
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.
Oligomerizationedit
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.
^Armstrong RN (1997). "Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases". Chemical Research in Toxicology. 10 (1): 2–18. doi:10.1021/tx960072x. 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". Journal of Biological Chemistry. 275 (32): 24798–24806. doi:10.1074/jbc.M001706200. PMID 10783391.
^Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P (2000). "The Glutathione Transferase Structural Family Includes a Nuclear Chloride Channel and a Ryanodine Receptor Calcium Release Channel Modulator". Journal of Biological Chemistry. 276 (5): 3319–3323. doi:10.1074/jbc.M007874200. PMID 11035031.
^Eaton DL, Bammler TK; Bammler (1999). "Concise review of the glutathione S-transferases and their significance to toxicology". Toxicological Sciences. 49 (2): 156–164. doi:10.1093/toxsci/49.2.156. PMID 10416260.
^Polekhina G, Board PG, Blackburn AC, Parker MW (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.
^Vuilleumier S (1997). "Bacterial glutathione S-transferases: What are they good for?". Journal of Bacteriology. 179 (5): 1431–1441. doi:10.1128/jb.179.5.1431-1441.1997. PMC178850. PMID 9045797.
Further readingedit
Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K (1998). "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles of Cys10 and His106". Journal of Molecular Biology. 281 (1): 135–147. doi:10.1006/jmbi.1998.1927. PMID 9680481.
Dixon DP, Lapthorn A, Edwards R (2002). "Plant glutathione transferases". Genome Biology. 3 (3): REVIEWS3004. doi:10.1186/gb-2002-3-3-reviews3004. PMC139027. PMID 11897031.
[1] 2008-12-05 at the Wayback Machine, GST Gene Fusion System Handbook by GE Healthcare Life Sciences
January 01, 1970
glutathione, transferase, terminal, domain, structural, domain, glutathione, transferase, identifierssymbolgst, cpfampf00043interproipr004046scop22gst, scope, supfamopm, superfamily131opm, protein1z9hcddcd00299available, protein, structures, pfam, structures, . Glutathione S transferase C terminal domain is a structural domain of glutathione S transferase GST Glutathione S transferase C terminal domainIdentifiersSymbolGST CPfamPF00043InterProIPR004046SCOP22gst SCOPe SUPFAMOPM superfamily131OPM protein1z9hCDDcd00299Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary 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 1 Biological function and classification 2 Oligomerization 3 Human proteins containing this domain 4 References 5 Further readingBiological function and classification editIn 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 editGlutathione 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 editEEF1E1 EEF1G GDAP1 GSTA1 GSTA2 GSTA3 GSTA4 GSTA5 GSTM1 GSTM2 GSTM3 GSTM4 GSTM5 GSTO1 GSTP1 GSTT1 GSTT2 GSTZ1 MARS PGDS PTGDS2 PTGES2 VARS References edit Armstrong RN 1997 Structure Catalytic Mechanism and Evolution of the Glutathione Transferases Chemical Research in Toxicology 10 1 2 18 doi 10 1021 tx960072x 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 Journal of Biological Chemistry 275 32 24798 24806 doi 10 1074 jbc M001706200 PMID 10783391 Dulhunty A Gage P Curtis S Chelvanayagam G Board P 2000 The Glutathione Transferase Structural Family Includes a Nuclear Chloride Channel and a Ryanodine Receptor Calcium Release Channel Modulator Journal of Biological Chemistry 276 5 3319 3323 doi 10 1074 jbc M007874200 PMID 11035031 Eaton DL Bammler TK Bammler 1999 Concise review of the glutathione S transferases and their significance to toxicology Toxicological Sciences 49 2 156 164 doi 10 1093 toxsci 49 2 156 PMID 10416260 Polekhina G Board PG Blackburn AC Parker MW 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 Vuilleumier S 1997 Bacterial glutathione S transferases What are they good for Journal of Bacteriology 179 5 1431 1441 doi 10 1128 jb 179 5 1431 1441 1997 PMC 178850 PMID 9045797 Further reading editNishida M Harada S Noguchi S Satow Y Inoue H Takahashi K 1998 Three dimensional structure of Escherichia coli glutathione S transferase complexed with glutathione sulfonate Catalytic roles of Cys10 and His106 Journal of Molecular Biology 281 1 135 147 doi 10 1006 jmbi 1998 1927 PMID 9680481 Dixon DP Lapthorn A Edwards R 2002 Plant glutathione transferases Genome Biology 3 3 REVIEWS3004 doi 10 1186 gb 2002 3 3 reviews3004 PMC 139027 PMID 11897031 1 Archived 2008 12 05 at the Wayback Machine GST Gene Fusion System Handbook by GE Healthcare Life Sciences Retrieved from https en wikipedia org w index php title Glutathione S transferase C terminal domain amp oldid 1188143368, wikipedia, wiki, book, books, library,
