Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 29, 2012, Pages 11693-11698

  Fyfe, Paul K ^a   Westrop, Gareth D ^b   Silva, Ana Marta ^b   Coombs, Graham H ^b   Hunter, William N ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b UNIVERSITY OF STRATHCLYDE   (United Kingdom)

Author keywords

Crystal structure; Protozoan biology; Redox metabolism; Thioltransferase

Indexed keywords

GLUTATHIONE TRANSFERASE; THIOL DEPENDENT REDUCTASE 1; UNCLASSIFIED DRUG;

ARTICLE; DEGLUTATHIONYLATION; ENZYME STRUCTURE; GENE DUPLICATION; GENE FUSION; GENETIC VARIABILITY; LEISHMANIA; NONHUMAN; PRIORITY JOURNAL; PROTEIN METABOLISM;

AMINO ACID SEQUENCE; ANTIMONY; BASE SEQUENCE; CRYSTALLOGRAPHY; EVOLUTION, MOLECULAR; GENES, DUPLICATE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; LEISHMANIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; POLYMERS; PRODRUGS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA;

PROTOZOA; TRYPANOSOMA CRUZI; TRYPANOSOMATIDAE;

EID: 84863884120     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1202593109     Document Type: Article

References (30)

1. Denton H, McGregor JC, Coombs GH (2004) Reduction of anti-leishmanial pentavalent antimonial drugs by a parasite-specific thiol-dependant reductase, TDR1. Biochem J 381:405-412. (Pubitemid 38969684)
2. Moutiez M, et al. (1997) Glutathione-dependent activities of Trypanosoma cruzi p52 makes it a new member of the thiol: Disulphide oxidoreductase family. Biochem J 322:43-48. (Pubitemid 27095520)
3. Olliaro PL, et al. (2005) Treatment options for visceral leishmaniasis: A systematic review of clinical studies done in India, 1980-2004. Lancet Infect Dis 5:763-774. (Pubitemid 41688981)
4. Ferreira CDS, et al. (2003) Thiol-induced reduction of antimony (V) into antimony (III): A comparative study with trypanothione, cysteinyl-glycine, cysteine and glutathione. Biometals 16:441-446.
5. Yan S, Li F, Ding K, Sun H (2003) Reduction of pentavalent antimony by trypanothione and formation of a binary and ternary complex of antimony (III) and trypanothione. J Biol Inorg Chem 8:689-697. (Pubitemid 36960817)
6. Shaked-Mishan P, Ulrich N, Ephros M, Zilberstein D (2001) Novel intracellular SbV reducing activity correlates with antimony susceptibility in Leishmania donovani. J Biol Chem 276:3971-3976.
7. Hayes JD, Flanagan JU, Jowsey IR (2005) Glutathione transferases. Annu Rev Pharmacol Toxicol 45:51-88. (Pubitemid 40261798)
8. Oakley AJ (2005) Glutathione transferases: New functions. Curr Opin Struct Biol 15:716-723.
9. Frova C (2006) Glutathione transferases in the genomics era: New insights and perspectives. Biomol Eng 23:149-169.
10. Tew KD, Townsend DM (2011) Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification. Drug Metab Rev 43:179-193.
11. Lillig CH, Berndt C, Holmgren A (2008) Glutaredoxin systems. Biochim Biophys Acta 1780:1304-1317.
12. Dirr H, Reinemer P, Huber R (1994) X-ray crystal structures of cytosolic glutathione S-transferases Implications for protein architecture, substrate recognition and catalytic function. Eur J Biochem 220:645-661. (Pubitemid 24107192)
13. Allocati N, et al. (2002) Glutamic acid-65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1. Biochem J 363:189-193. (Pubitemid 34280626)
14. Kortemme T, Creighton TE (1995) Ionisation of cysteine residues at the termini of model α-helical peptides; relevance to unusual thiol pKa values in proteins of the thioredoxin family. J Mol Biol 253:799-812.
15. Board PG, et al. (2000) Identification, characterization, and crystal structure of the omega class glutathione transferases. J Biol Chem 275:24798-24806. (Pubitemid 30626584)
16. Ceylan S, et al. (2010) The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism. J Biol Chem 285:35224-35237.
17. Krauth-Siegel RL, Comini MA (2008) Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism. Biochim Biophys Acta 1780:1236-1248.
18. Alphey MS, et al. (1999) The high-resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I. J Biol Chem 274:25613-25622.
19. Garcerá A, Barreto L, Piedrafita L, Tamarit J, Herrero E (2006) Saccharomyces cerevisiae cells have three omega class glutathione S-transferases acting as 1-Cys thiol transferases. Biochem J 398:187-196. (Pubitemid 44338475)
20. Johansson C, Lillig CH, Holmgren A (2004) Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem 279:7537-7543. (Pubitemid 38294632)
21. Peltoniemi MJ, Karala AR, Jurvansuu JK, Kinnula VL, Ruddock LW (2006) Insights into deglutathionylation reactions: Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the γ-linkage present in glutathione. J Biol Chem 281:33107-33114. (Pubitemid 46036692)
22. Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ (2001) Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases. J Mol Biol 310:907-918. (Pubitemid 32695704)
23. Bonilla M, Denicola A, Marino SM, Gladyshev VN, Salinas G (2011) Linked thioredoxinglutathione systems in platyhelminth parasites: Alternative pathways for glutathione reduction and deglutathionylation. J Biol Chem 286:4959-4967.
24. Dalle-Donne I, et al. (2008) S-glutathiolation in life and death decisions of the cell. Free Radic Res 45:3-15.
25. Shelton MD, Mieyal JJ (2008) Regulation by reversible S-glutathionylation: Molecular targets implicated in inflammatory diseases. Mol Cells 25:332-346.
26. Bond CS, White MF, Hunter WN (2001) High-resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase. J Biol Chem 276:3247-3253. (Pubitemid 37411618)
27. Dawson A, Fyfe PK, Hunter WN (2008) Specificity and reactivity in menaquinone biosynthesis; the structure of Escherichia coli MenD [2-succinyl-5-enolpyruvyl-6-hydroxy- 3-cyclohexadiene-1-carboxylate synthase]. J Mol Biol 384:1353-1368.
28. Edgar RC (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797.
29. Drummond AJ, Rambaut A (2007) BEAST: Bayesian evolutionary analysis by sampling trees. BMC Evol Biol 7:214.
30. Bond CS, Schüttelkopf AW (2009) ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr D Biol Crystallogr D65:510-512.