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Q8MU52

- GST_PLAFA

UniProt

Q8MU52 - GST_PLAFA

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Protein

Glutathione S-transferase

Gene

GST

Organism
Plasmodium falciparum
Status
Reviewed - 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

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

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 – 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
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.
DrugBanki DB00608. Chloroquine.

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: November 26, 2014
This is version 69 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