Q8MU52 (GST_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase
EC=2.5.1.18

Alternative name(s):
PfGST

Gene names

Name:

GST

Organism

Plasmodium falciparum

Taxonomic identifier

5833 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Transferase
Technical term	3D-structure
Gene Ontology (GO)
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 211

211

Glutathione S-transferase

PRO_0000259966

Regions

Domain

3 – 87

85

GST N-terminal

Domain

89 – 211

123

GST C-terminal

Region

58 – 59

2

Glutathione binding

Region

71 – 72

2

Glutathione binding

Sites

Binding site

9

1

Glutathione

Experimental info

Mutagenesis

9

1

Y → F: Greater than 10-fold decrease in activity. Ref.6

Mutagenesis

15

1

K → E: 10-fold decrease in substrate affinity and 20-fold decrease in activity. Ref.6

Mutagenesis

71

1

Q → E: 3-fold decrease in substrate affinity and 2-fold decrease in activity. Ref.6

Mutagenesis

101

1

C → A: 2-fold decrease in substrate affinity. Ref.6

Mutagenesis

211

1

Y → F: 2-fold increase in activity. Ref.6

Sequence conflict

1

1

M → MKL in AAL25087. Ref.2

Secondary structure

1

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211

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Turn

14 – 16

3

Helix

17 – 26

10

Beta strand

31 – 35

5

Beta strand

37 – 39

3

Helix

41 – 51

11

Beta strand

55 – 57

3

Beta strand

61 – 64

4

Beta strand

67 – 70

4

Helix

72 – 82

11

Helix

90 – 110

21

Turn

115 – 118

4

Helix

120 – 125

6

Helix

127 – 141

15

Turn

142 – 144

3

Helix

160 – 173

14

Turn

179 – 182

4

Helix

184 – 194

11

Helix

197 – 205

9

Sequences

	Sequence		Length	Mass (Da)
	Q8MU52 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: EDC79583CFC9D751	FASTA	211	24,789
	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

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

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	[»]

ProteinModelPortal

Q8MU52.

SMR

Q8MU52. Positions 1-211.

ModBase

Search...

Proteomic databases

PRIDE

Q8MU52.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

NOG05174.

Enzyme and pathway databases

SABIO-RK

Q8MU52.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q8MU52.

ChEMBL

CHEMBL1697656.

EvolutionaryTrace

Q8MU52.

Entry information

Entry name

GST_PLAFA

Accession

Primary (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 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)