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Protein

Glutathione S-transferase

Gene

GST

Organism
Plasmodium falciparum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).3 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.4 Publications

Enzyme regulationi

Inhibited by chloroquine, cibacron blue, ferriprotoporphyrin IX (hemin) and S-hexylglutathione.3 Publications

Kineticsi

  1. KM=0.156 mM for bromosulphophthalein4 Publications
  2. KM=10 mM for 1-chloro-2,4-dinitrobenzene4 Publications
  3. KM=2.5 mM for 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole4 Publications
  4. KM=0.96 mM for ethacrynic acid4 Publications
  5. KM=0.164 mM for reduced glutathione4 Publications

    pH dependencei

    Optimum pH is 8.1.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Glutathione

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4889.
    SABIO-RKQ8MU52.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase (EC:2.5.1.18)
    Alternative name(s):
    PfGST
    Gene namesi
    Name:GST
    OrganismiPlasmodium falciparum
    Taxonomic identifieri5833 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91Y → F: Greater than 10-fold decrease in activity. 1 Publication
    Mutagenesisi15 – 151K → E: 10-fold decrease in substrate affinity and 20-fold decrease in activity. 1 Publication
    Mutagenesisi71 – 711Q → E: 3-fold decrease in substrate affinity and 2-fold decrease in activity. 1 Publication
    Mutagenesisi101 – 1011C → A: 2-fold decrease in substrate affinity. 1 Publication
    Mutagenesisi211 – 2111Y → F: 2-fold increase in activity. 1 Publication

    Chemistry

    DrugBankiDB00608. Chloroquine.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Glutathione S-transferasePRO_0000259966Add
    BLAST

    Proteomic databases

    PRIDEiQ8MU52.

    Interactioni

    Subunit structurei

    Homodimer. In the absence of ligands two homodimers may interact to form a tetramer.2 Publications

    Protein-protein interaction databases

    STRINGi5833.PF14_0187.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139Combined sources
    Turni14 – 163Combined sources
    Helixi17 – 2610Combined sources
    Beta strandi31 – 355Combined sources
    Beta strandi37 – 393Combined sources
    Helixi41 – 5111Combined sources
    Beta strandi55 – 573Combined sources
    Beta strandi61 – 644Combined sources
    Beta strandi67 – 704Combined sources
    Helixi72 – 8211Combined sources
    Helixi90 – 11021Combined sources
    Turni115 – 1184Combined sources
    Helixi120 – 1256Combined sources
    Helixi127 – 14115Combined sources
    Turni142 – 1443Combined sources
    Helixi160 – 17314Combined sources
    Turni179 – 1824Combined sources
    Helixi184 – 19411Combined sources
    Helixi197 – 2059Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OKTX-ray1.90A/B1-211[»]
    1PA3X-ray2.70A/B1-211[»]
    1Q4JX-ray2.20A/B1-211[»]
    2AAWX-ray2.40A/C1-211[»]
    3FR3X-ray1.90A/B1-211[»]
    3FR6X-ray2.60A/B1-211[»]
    3FR9X-ray2.40A/B1-211[»]
    3FRCX-ray2.00A/B1-211[»]
    ProteinModelPortaliQ8MU52.
    SMRiQ8MU52. Positions 1-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8MU52.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8785GST N-terminalAdd
    BLAST
    Domaini89 – 211123GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 592Glutathione binding
    Regioni71 – 722Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiNOG05174.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8MU52-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGDNIVLYYF DARGKAELIR LIFAYLGIEY TDKRFGVNGD AFVEFKNFKK
    60 70 80 90 100
    EKDTPFEQVP ILQIGDLILA QSQAIVRYLS KKYNICGESE LNEFYADMIF
    110 120 130 140 150
    CGVQDIHYKF NNTNLFKQNE TTFLNEDLPK WSGYFEKLLK KNHTNNNNDK
    160 170 180 190 200
    YYFVGNNLTY ADLAVFNLYD DIETKYPSSL KNFPLLKAHN EFISNLPNIK
    210
    NYITNRKESV Y
    Length:211
    Mass (Da):24,789
    Last modified:October 1, 2002 - v1
    Checksum:iEDC79583CFC9D751
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → MKL in AAL25087 (PubMed:12387854).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY014840 mRNA. Translation: AAK00582.1.
    AF426836 mRNA. Translation: AAL25087.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY014840 mRNA. Translation: AAK00582.1.
    AF426836 mRNA. Translation: AAL25087.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OKTX-ray1.90A/B1-211[»]
    1PA3X-ray2.70A/B1-211[»]
    1Q4JX-ray2.20A/B1-211[»]
    2AAWX-ray2.40A/C1-211[»]
    3FR3X-ray1.90A/B1-211[»]
    3FR6X-ray2.60A/B1-211[»]
    3FR9X-ray2.40A/B1-211[»]
    3FRCX-ray2.00A/B1-211[»]
    ProteinModelPortaliQ8MU52.
    SMRiQ8MU52. Positions 1-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5833.PF14_0187.

    Chemistry

    BindingDBiQ8MU52.
    ChEMBLiCHEMBL1697656.
    DrugBankiDB00608. Chloroquine.

    Proteomic databases

    PRIDEiQ8MU52.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiNOG05174.

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4889.
    SABIO-RKQ8MU52.

    Miscellaneous databases

    EvolutionaryTraceiQ8MU52.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Glutathione S-transferase of the malarial parasite Plasmodium falciparum: characterization of a potential drug target."
      Harwaldt P., Rahlfs S., Becker K.
      Biol. Chem. 383:821-830(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SELF-ASSOCIATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SELF-ASSOCIATION.
    3. "Cooperativity and pseudo-cooperativity in the glutathione S-transferase from Plasmodium falciparum."
      Liebau E., De Maria F., Burmeister C., Perbandt M., Turella P., Antonini G., Federici G., Giansanti F., Stella L., Lo Bello M., Caccuri A.M., Ricci G.
      J. Biol. Chem. 280:26121-26128(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum."
      Fritz-Wolf K., Becker A., Rahlfs S., Harwaldt P., Schirmer R.H., Kabsch W., Becker K.
      Proc. Natl. Acad. Sci. U.S.A. 100:13821-13826(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY.
    5. "Native and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparum."
      Perbandt M., Burmeister C., Walter R.D., Betzel C., Liebau E.
      J. Biol. Chem. 279:1336-1342(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH S-HEXYL GLUTATHIONE.
    6. "Plasmodium falciparum glutathione S-transferase -- structural and mechanistic studies on ligand binding and enzyme inhibition."
      Hiller N., Fritz-Wolf K., Deponte M., Wende W., Zimmermann H., Becker K.
      Protein Sci. 15:281-289(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH S-HEXYL GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SELF-ASSOCIATION, MUTAGENESIS OF TYR-9; LYS-15; GLN-71; CYS-101 AND TYR-211.

    Entry informationi

    Entry nameiGST_PLAFA
    AccessioniPrimary (citable) accession number: Q8MU52
    Secondary accession number(s): Q95V54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: October 1, 2002
    Last modified: June 24, 2015
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.