GST26_SCHJA
ID GST26_SCHJA Reviewed; 218 AA.
AC P08515;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme;
DE Short=GST 26;
DE EC=2.5.1.18;
DE AltName: Full=Sj26 antigen;
DE AltName: Full=SjGST;
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3095841; DOI=10.1073/pnas.83.22.8703;
RA Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.;
RT "Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI
RT 129/J mice is a parasite glutathione S-transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8703-8707(1986).
RN [2]
RP SEQUENCE REVISION.
RA Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.;
RL Proc. Natl. Acad. Sci. U.S.A. 84:6541-6541(1987).
RN [3]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=3278228; DOI=10.1016/0166-6851(88)90044-8;
RA Smith D.B., Rubira M.R., Simpson R.J., Davern K.M., Tiu W.U., Board P.G.,
RA Mitchell G.F.;
RT "Expression of an enzymatically active parasite molecule in Escherichia
RT coli: Schistosoma japonicum glutathione S-transferase.";
RL Mol. Biochem. Parasitol. 27:249-256(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX PubMed=7538846; DOI=10.1002/pro.5560031209;
RA Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C.;
RT "Three-dimensional structure of Schistosoma japonicum glutathione S-
RT transferase fused with a six-amino acid conserved neutralizing epitope of
RT gp41 from HIV.";
RL Protein Sci. 3:2233-2244(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP PRAZIQUANTEL.
RX PubMed=7853399; DOI=10.1006/jmbi.1994.0061;
RA McTigue M.A., Williams D.R., Tainer J.A.;
RT "Crystal structures of a schistosomal drug and vaccine target: glutathione
RT S-transferase from Schistosoma japonica and its complex with the leading
RT antischistosomal drug praziquantel.";
RL J. Mol. Biol. 246:21-27(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE
RP ANALOGS.
RX PubMed=12596270; DOI=10.1002/prot.10345;
RA Cardoso R.M., Daniels D.S., Bruns C.M., Tainer J.A.;
RT "Characterization of the electrophile binding site and substrate binding
RT mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum.";
RL Proteins 51:137-146(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-214.
RX PubMed=19177365; DOI=10.1002/pro.23;
RA Sagermann M., Chapleau R.R., DeLorimier E., Lei M.;
RT "Using affinity chromatography to engineer and characterize pH-dependent
RT protein switches.";
RL Protein Sci. 18:217-228(2009).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC -!- FUNCTION: GST isoenzymes appear to play a central role in the parasite
CC detoxification system. Other functions are also suspected including a
CC role in increasing the solubility of haematin in the parasite gut.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7853399}.
CC -!- MISCELLANEOUS: There are at least two isoenzymes of GST in S.japonicum.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; M14654; AAB59203.1; -; mRNA.
DR PIR; A61514; A61514.
DR PDB; 1B8X; X-ray; 2.70 A; A=2-218.
DR PDB; 1BG5; X-ray; 2.60 A; A=1-218.
DR PDB; 1DUG; X-ray; 1.80 A; A/B=2-218.
DR PDB; 1GNE; X-ray; 2.50 A; A=2-218.
DR PDB; 1GTA; X-ray; 2.40 A; A=1-218.
DR PDB; 1GTB; X-ray; 2.60 A; A=1-218.
DR PDB; 1M99; X-ray; 2.30 A; A=1-218.
DR PDB; 1M9A; X-ray; 2.10 A; A=1-218.
DR PDB; 1M9B; X-ray; 2.60 A; A=1-218.
DR PDB; 1U87; X-ray; 3.50 A; A=1-218.
DR PDB; 1U88; X-ray; 3.50 A; A/B=1-218.
DR PDB; 1UA5; X-ray; 2.50 A; A=1-218.
DR PDB; 1Y6E; X-ray; 3.00 A; A/B=2-218.
DR PDB; 3CRT; X-ray; 1.90 A; A=1-214.
DR PDB; 3CRU; X-ray; 2.30 A; A=1-214.
DR PDB; 3D0Z; X-ray; 2.50 A; A=1-214.
DR PDB; 3QMZ; X-ray; 6.00 A; S/T=2-218.
DR PDB; 4AI6; X-ray; 3.40 A; A/B=2-218.
DR PDB; 4AKG; X-ray; 3.30 A; A/B=2-218.
DR PDB; 4AKH; X-ray; 3.60 A; A/B=2-218.
DR PDB; 4AKI; X-ray; 3.70 A; A/B=2-218.
DR PDB; 4ECB; X-ray; 2.20 A; A/B=1-218.
DR PDB; 4ECC; X-ray; 2.20 A; A=1-215.
DR PDB; 4WR4; X-ray; 1.60 A; A=2-218.
DR PDB; 4WR5; X-ray; 1.93 A; A=2-218.
DR PDB; 5GZZ; X-ray; 2.39 A; B/C/D/E/F/G=1-218.
DR PDB; 6JI6; X-ray; 1.50 A; A=1-218.
DR PDB; 6N8U; X-ray; 1.96 A; A/B=1-218.
DR PDB; 6RWD; X-ray; 1.53 A; A/B=1-218.
DR PDB; 7NT8; X-ray; 2.22 A; A/B=1-218.
DR PDBsum; 1B8X; -.
DR PDBsum; 1BG5; -.
DR PDBsum; 1DUG; -.
DR PDBsum; 1GNE; -.
DR PDBsum; 1GTA; -.
DR PDBsum; 1GTB; -.
DR PDBsum; 1M99; -.
DR PDBsum; 1M9A; -.
DR PDBsum; 1M9B; -.
DR PDBsum; 1U87; -.
DR PDBsum; 1U88; -.
DR PDBsum; 1UA5; -.
DR PDBsum; 1Y6E; -.
DR PDBsum; 3CRT; -.
DR PDBsum; 3CRU; -.
DR PDBsum; 3D0Z; -.
DR PDBsum; 3QMZ; -.
DR PDBsum; 4AI6; -.
DR PDBsum; 4AKG; -.
DR PDBsum; 4AKH; -.
DR PDBsum; 4AKI; -.
DR PDBsum; 4ECB; -.
DR PDBsum; 4ECC; -.
DR PDBsum; 4WR4; -.
DR PDBsum; 4WR5; -.
DR PDBsum; 5GZZ; -.
DR PDBsum; 6JI6; -.
DR PDBsum; 6N8U; -.
DR PDBsum; 6RWD; -.
DR PDBsum; 7NT8; -.
DR AlphaFoldDB; P08515; -.
DR SASBDB; P08515; -.
DR SMR; P08515; -.
DR DrugCentral; P08515; -.
DR PRIDE; P08515; -.
DR ABCD; P08515; 23 sequenced antibodies.
DR BRENDA; 2.5.1.18; 5607.
DR EvolutionaryTrace; P08515; -.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3278228"
FT CHAIN 2..218
FT /note="Glutathione S-transferase class-mu 26 kDa isozyme"
FT /id="PRO_0000185805"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT DOMAIN 85..203
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:7538846,
FT ECO:0000305|PubMed:12596270"
FT BINDING 41..45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:7538846,
FT ECO:0000305|PubMed:12596270"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:7538846,
FT ECO:0000305|PubMed:12596270"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:7538846,
FT ECO:0000305|PubMed:12596270"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:6JI6"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:6N8U"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4WR5"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6JI6"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 86..110
FT /evidence="ECO:0007829|PDB:6JI6"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 115..136
FT /evidence="ECO:0007829|PDB:6JI6"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6JI6"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:6JI6"
FT TURN 167..172
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:6JI6"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:6JI6"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1GTA"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1BG5"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6JI6"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6RWD"
SQ SEQUENCE 218 AA; 25499 MW; 5E2AC418BD0EF13F CRC64;
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID
GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV
DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK
KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK
