The structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 6, 2014, Pages 1517-1527

  Chitnumsub, Penchit ^a   Ittarat, Wanwipa ^a   Jaruwat, Aritsara ^a   Noytanom, Krittikar ^a   Amornwatcharapong, Watcharee ^b   Pornthanakasem, Wichai ^a   Chaiyen, Pimchai ^b   Yuthavong, Yongyuth ^a   Leartsakulpanich, Ubolsree ^a  

^a NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

^b Mahidol University   (Thailand)

Author keywords

antimalarial target; disulfide sulfhydryl switch; Plasmodium falciparum; protein engineering; serine hydroxymethyltransferase

Indexed keywords

GLYCINE HYDROXYMETHYLTRANSFERASE;

AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PLASMODIUM FALCIPARUM; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; ULTRAVIOLET SPECTROPHOTOMETRY; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLIZATION; GLYCINE HYDROXYMETHYLTRANSFERASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PLASMODIUM FALCIPARUM; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURE-ACTIVITY RELATIONSHIP; X-RAY DIFFRACTION;

EID: 84902492777     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714005598     Document Type: Article

References (45)

1. Amadasi, A., Bertoldi, M., Contestabile, R., Bettati, S., Cellini, B., di Salvo, M. L., Borri-Voltattorni, C., Bossa, F. & Mozzarelli, A. (2007). Curr. Med. Chem. 14, 1291-1324.
2. Bradford, M. M. (1976). Anal. Biochem. 72, 248-254.
3. Chayen, N. E. (1996). Protein Eng. 9, 927-929.
4. Chitnumsub, P., Yavaniyama, J., Vanichtanankul, J., Kamchonwongpaisan, S., Walkinshaw, M. D. & Yuthavong, Y. (2004). Acta Cryst. D60, 780-783.
5. Choi, H., Kim, S., Mukhopadhyay, P., Cho, S., Woo, J., Storz, G. & Ryu, S.-E. (2001). Cell, 105, 103-113.
6. D'Arcy, A., Elmore, C., Stihle, M. & Johnston, J. E. (1996). J. Cryst. Growth, 168, 175-180.
7. Dunathan, H. C. (1966). Proc. Natl Acad. Sci. USA, 55, 712-716.
8. Eliot, A. C. & Kirsch, J. F. (2004). Annu. Rev. Biochem. 73, 383-415.
9. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
10. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
11. Evdokimov, A. G. et al. (2008). J. Struct. Biol. 162, 152-169.
12. Fass, D. (2012). Annu. Rev. Biophys. 41, 63-79.
13. Fu, T.-F., Scarsdale, J. N., Kazanina, G., Schirch, V. & Wright, H. T. (2003). J. Biol. Chem. 278, 2645-2653.
14. Kleywegt, G. J. (1996). Acta Cryst. D52, 842-857.
15. Lambert, C., Léonard, N., De Bolle, X. & Depiereux, E. (2002). Bioinformatics, 18, 1250-1256.
16. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
17. Liu, X., Reig, B., Nasrallah, I. M. & Stover, P. J. (2000). Biochemistry, 39, 11523-11531.
18. Liu, W., Wen, W., Wei, Z., Yu, J., Ye, F., Liu, C.-H., Hardie, R. C. & Zhang, M. (2011). Cell, 145, 1088-1101.
19. Maenpuen, S., Sopitthummakhun, K., Yuthavong, Y., Chaiyen, P. & Leartsakulpanich, U. (2009). Mol. Biochem. Parasitol. 168, 63-73.
20. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C. & Read, R. J. (2007). J. Appl. Cryst. 40, 658-674.
21. Mozzarelli, A. & Bettati, S. (2006). Chem. Rec. 6, 275-287.
22. Müller, I. B. & Hyde, J. E. (2013). Mol. Biochem. Parasitol. 188, 63-77.
23. Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
24. Navaza, J. (1994). Acta Cryst. A50, 157-163.
25. Nirmalan, N., Wang, P., Sims, P. F. & Hyde, J. E. (2002). Mol. Microbiol. 46, 179-190.
26. Otwinowski, Z. & Minor,W. (1997). Methods Enzymol. 276, 307-326.
27. Pang, C. K. T., Hunter, J. H., Gujjar, R., Podutoori, R., Bowman, J., Mudeppa, D. G. & Rathod, P. K. (2009). Mol. Biochem. Parasitol. 168, 74-83.
28. Pornthanakasem, W., Kongkasuriyachai, D., Uthaipibull, C., Yuthavong, Y. & Leartsakulpanich, U. (2012). Malar. J. 11, 387.
29. Rao, D. N. & Rao, N. A. (1980). Biochem. Biophys. Res. Commun. 92, 1166-1171.
30. Reddie, K. G. & Carroll, K. S. (2008). Curr. Opin. Chem. Biol. 12, 746-754.
31. Renwick, S. B., Snell, K. & Baumann, U. (1998). Structure, 6, 1105-1116.
32. Ryu, S.-E. (2012). J. Biochem. 151, 579-588.
33. Scarsdale, J. N., Radaev, S., Kazanina, G., Schirch, V. & Wright, H. T. (2000). J. Mol. Biol. 296, 155-168.
34. Schirch, V. (1998). Comprehensive Biological Catalysis, edited by M. Sinnott, Vol. 1, pp. 211-252.
35. San Diego: Academic Press. Schirch, V. & Szebenyi, D. M. (2005). Curr. Opin. Chem. Biol. 9, 482-487.
36. Sopitthummakhun, K., Maenpuen, S., Yuthavong, Y., Leartsakulpanich, U. & Chaiyen, P. (2009). FEBS J. 276, 4023-4036.
37. Sopitthummakhun, K., Thongpanchang, C., Vilaivan, T., Yuthavong, Y., Chaiyen, P. & Leartsakulpanich, U. (2012). Malar. J. 11, 194.
38. Szebenyi, D. M., Liu, X., Kriksunov, I. A., Stover, P. J. & Thiel, D. J. (2000). Biochemistry, 39, 13313-13323.
39. Toledano, M. B., Kullik, I., Trinh, F., Baird, P. T., Schneider, T. D. & Storz, G. (1994). Cell, 78, 897-909.
40. Toney, M. D. (2005). Arch. Biochem. Biophys. 433, 279-287.
41. Trivedi, V., Gupta, A., Jala, V. R., Saravanan, P., Rao, G. S., Rao, N. A., Savithri, H. S. & Subramanya, H. S. (2002). J. Biol. Chem. 277, 17161-17169.
42. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
43. World Health Organization (2012). World Malaria Report 2012. Geneva: World Health Organization. http://www.who.int/malaria/ publications/world- malaria-report-2012/en/.
44. Zheng, M., Aslund, F. & Storz, G. (1998). Science, 279, 1718-1721.
45. Zhou, A., Carrell, R. W., Murphy, M. P., Wei, Z., Yan, Y., Stanley, P. L., Stein, P. E., Broughton Pipkin, F. & Read, R. J. (2010). Nature (London), 468, 108-111.