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Q8MU52 (GST_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase

EC=2.5.1.18
Alternative name(s):
PfGST
Gene names
Name:GST
OrganismPlasmodium falciparum
Taxonomic identifier5833 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.2 Ref.6

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.1 Ref.2 Ref.3 Ref.4

Enzyme regulation

Inhibited by chloroquine, cibacron blue, ferriprotoporphyrin IX (hemin) and S-hexylglutathione. Ref.1 Ref.2 Ref.3

Subunit structure

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

Sequence similarities

Belongs to the GST superfamily.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.156 mM for bromosulphophthalein Ref.1 Ref.2 Ref.3 Ref.6

KM=10 mM for 1-chloro-2,4-dinitrobenzene

KM=2.5 mM for 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole

KM=0.96 mM for ethacrynic acid

KM=0.164 mM for reduced glutathione

pH dependence:

Optimum pH is 8.1.

Ontologies

Keywords
   Molecular functionTransferase
   Technical term3D-structure
Gene Ontology (GO)
   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Glutathione S-transferase
PRO_0000259966

Regions

Domain3 – 8785GST N-terminal
Domain89 – 211123GST C-terminal
Region58 – 592Glutathione binding
Region71 – 722Glutathione binding

Sites

Binding site91Glutathione

Experimental info

Mutagenesis91Y → F: Greater than 10-fold decrease in activity. Ref.6
Mutagenesis151K → E: 10-fold decrease in substrate affinity and 20-fold decrease in activity. Ref.6
Mutagenesis711Q → E: 3-fold decrease in substrate affinity and 2-fold decrease in activity. Ref.6
Mutagenesis1011C → A: 2-fold decrease in substrate affinity. Ref.6
Mutagenesis2111Y → F: 2-fold increase in activity. Ref.6
Sequence conflict11M → MKL in AAL25087. Ref.2

Secondary structure

.................................... 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8MU52 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: EDC79583CFC9D751

FASTA21124,789
        10         20         30         40         50         60 
MGDNIVLYYF DARGKAELIR LIFAYLGIEY TDKRFGVNGD AFVEFKNFKK EKDTPFEQVP 

        70         80         90        100        110        120 
ILQIGDLILA QSQAIVRYLS KKYNICGESE LNEFYADMIF CGVQDIHYKF NNTNLFKQNE 

       130        140        150        160        170        180 
TTFLNEDLPK WSGYFEKLLK KNHTNNNNDK YYFVGNNLTY ADLAVFNLYD DIETKYPSSL 

       190        200        210 
KNFPLLKAHN EFISNLPNIK NYITNRKESV Y 

« Hide

References

[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]"The glutathione S-transferase from Plasmodium falciparum."
Liebau E., Bergmann B., Campbell A.M., Teesdale-Spittle P., Brophy P.M., Lueersen K., Walter R.D.
Mol. Biochem. Parasitol. 124:85-90(2002) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY014840 mRNA. Translation: AAK00582.1.
AF426836 mRNA. Translation: AAL25087.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ8MU52.
SMRQ8MU52. Positions 1-211.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ8MU52.
ChEMBLCHEMBL1697656.

Proteomic databases

PRIDEQ8MU52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG05174.

Enzyme and pathway databases

SABIO-RKQ8MU52.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8MU52.

Entry information

Entry nameGST_PLAFA
AccessionPrimary (citable) accession number: Q8MU52
Secondary accession number(s): Q95V54
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references