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Q8MU52

- GST_PLAFA

UniProt

Q8MU52 - GST_PLAFA

Protein

Glutathione S-transferase

Gene

GST

Organism
Plasmodium falciparum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    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

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    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 lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (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

    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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MGDNIVLYYF DARGKAELIR LIFAYLGIEY TDKRFGVNGD AFVEFKNFKK    50
    EKDTPFEQVP ILQIGDLILA QSQAIVRYLS KKYNICGESE LNEFYADMIF 100
    CGVQDIHYKF NNTNLFKQNE TTFLNEDLPK WSGYFEKLLK KNHTNNNNDK 150
    YYFVGNNLTY ADLAVFNLYD DIETKYPSSL KNFPLLKAHN EFISNLPNIK 200
    NYITNRKESV Y 211
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY014840 mRNA. Translation: AAK00582.1.
    AF426836 mRNA. Translation: AAL25087.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY014840 mRNA. Translation: AAK00582.1 .
    AF426836 mRNA. Translation: AAL25087.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OKT X-ray 1.90 A/B 1-211 [» ]
    1PA3 X-ray 2.70 A/B 1-211 [» ]
    1Q4J X-ray 2.20 A/B 1-211 [» ]
    2AAW X-ray 2.40 A/C 1-211 [» ]
    3FR3 X-ray 1.90 A/B 1-211 [» ]
    3FR6 X-ray 2.60 A/B 1-211 [» ]
    3FR9 X-ray 2.40 A/B 1-211 [» ]
    3FRC X-ray 2.00 A/B 1-211 [» ]
    ProteinModelPortali Q8MU52.
    SMRi Q8MU52. Positions 1-211.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q8MU52.
    ChEMBLi CHEMBL1697656.

    Proteomic databases

    PRIDEi Q8MU52.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG05174.

    Enzyme and pathway databases

    SABIO-RK Q8MU52.

    Miscellaneous databases

    EvolutionaryTracei Q8MU52.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF14497. GST_C_3. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 67 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