High-resolution structures of Thermus thermophilus enoyl-acyl carrier protein reductase in the apo form, in complex with NAD+ and in complex with NAD+ and triclosan

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 10, 2012, Pages 1139-1148

  Otero, José M ^a   Nol, Ann Josée ^b   Guardado Calvo, Pablo ^a,c   Llamas Saiz, Antonio L ^a   Wende, Wolfgang ^b   Schierling, Benno ^b   Pingoud, Alfred ^b   Van Raaij, Mark J ^a,d  

^a UNIVERSITY OF SANTIAGO DE COMPOSTELA   (Spain)

^b JUSTUS LIEBIG UNIVERSITY   (Germany)

^c INSTITUT PASTEUR   (France)

^d CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

Author keywords

enoyl acyl carrier protein reductases; fatty acid synthesis; Thermus thermophilus; triclosan

Indexed keywords

APOENZYME; ENOYL ACYL CARRIER PROTEIN REDUCTASE (NADH); NICOTINAMIDE ADENINE DINUCLEOTIDE; TRICLOSAN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; APOENZYMES; ENOYL-(ACYL-CARRIER-PROTEIN) REDUCTASE (NADH); ENZYME STABILITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NAD; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN; THERMUS THERMOPHILUS; TRICLOSAN;

EID: 84867257936     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112033982     Document Type: Article

References (38)

1. Baldock, C., Rafferty, J. B., Sedelnikova, S. E., Baker, P. J., Stuitje, A. R., Slabas, A. R., Hawkes, T. R. & Rice, D. W. (1996). Science, 274, 2107-2110.
2. Bergler, H., Wallner, P., Ebeling, A., Leitinger, B., Fuchsbichler, S., Aschauer, H., Kollenz, G., Hogenauer, G. & Turnowsky, F. (1994). J. Biol. Chem. 269, 5493-5496.
3. Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Cryst. D66, 12-21.
4. Dessen, A., Que'mard, A., Blanchard, J. S., Jacobs, W. R. & Sacchettini, J. C. (1995). Science, 267, 1638-1641.
5. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
6. Evans, P. (2006). Acta Cryst. D62, 72-82.
7. Kim, K.-H., Ha, B. H., Kim, S. J., Hong, S. K., Hwang, K. Y. & Kim, E. E. (2011). J. Mol. Biol. 406, 403-415.
8. Kim, S. J., Ha, B. H., Kim, K.-H., Hong, S. K., Shin, K.-J., Suh, S. W. & Kim, E. E. (2010). Biochem. Biophys. Res. Commun. 400, 517-522.
9. Krissinel, E. & Henrick, K. (2007). J. Mol. Biol. 372, 774-797.
10. Kumar, S., Tsai, C.-J. & Nussinov, R. (2000). Protein Eng. 13, 179-191.
11. Kuo, M. R. et al. (2003). J. Biol. Chem. 278, 20851-20859.
12. Laemmli, U. K. (1970). Nature (London), 227, 680-685.
13. Lee, H. H., Moon, J. & Suh, S. W. (2007). Proteins, 69, 691-694.
14. Leibundgut, M., Maier, T., Jenni, S. & Ban, N. (2008). Curr. Opin. Struct. Biol. 18, 714-725.
15. Leslie, A. G. W. (2006). Acta Cryst. D62, 48-57.
16. Levy, C. W., Roujeinikova, A., Sedelnikova, S., Baker, P. J., Stuitje, A. R., Slabas, A. R., Rice, D. W. & Rafferty, J. B. (1999). Nature (London), 398, 383-384.
17. Lu, H., England, K., am Ende, C., Truglio, J. J., Luckner, S., Reddy, B. G., Marlenee, N. L., Knudson, S. E., Knudson, D. L., Bowen, R. A., Kisker, C., Slayden, R. A. & Tonge, P. J. (2009). ACS Chem. Biol. 4, 221-231.
18. Lu, J. Z., Muench, S. P., Allary, M., Campbell, S., Roberts, C. W., Mui, E., McLeod, R. L., Rice, D. W. & Prigge, S. T. (2007). Parasitology, 134, 1949-1962.
19. Massengo-Tiassé, R. P. & Cronan, J. E. (2009). Cell. Mol. Life Sci. 66, 1507-1517.
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. Muench, S. P., Prigge, S. T., McLeod, R., Rafferty, J. B., Kirisits, M. J., Roberts, C. W., Mui, E. J. & Rice, D. W. (2007). Acta Cryst. D63, 328-338.
22. Murshudov, G. N., Skubá k, 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.
23. Nayal, M. & Di Cera, E. (1996). J. Mol. Biol. 256, 228-234.
24. Oshima, T. (1974). Seikagaku, 46, 887-907.
25. Perozzo, R., Kuo, M., Sidhu, A. S., Valiyaveettil, J. T., Bittman, R., Jacobs, W. R., Fidock, D. A. & Sacchettini, J. C. (2002). J. Biol. Chem. 277, 13106-13114.
26. Pidugu, L. S., Kapoor, M., Surolia, N., Surolia, A. & Suguna, K. (2004). J. Mol. Biol. 343, 147-155.
27. Powell, H. R. (1999). Acta Cryst. D55, 1690-1695.
28. Priyadarshi, A., Kim, E. E. & Hwang, K. Y. (2010). Proteins, 78, 480-486.
29. Qiu, X., Janson, C. A., Court, R. I., Smyth, M. G., Payne, D. J. & Abdel-Meguid, S. S. (1999). Protein Sci. 8, 2529-2532.
30. Rafi, S., Novichenok, P., Kolappan, S., Zhang, X., Stratton, C. F., Rawat, R., Kisker, C., Simmerling, C. & Tonge, P. J. (2006). J. Biol. Chem. 281, 39285-39293.
31. Rossmann, M. G., Liljas, A., Granden, G. & Baraszak, L. (1975). The Enzymes, 3rd ed., edited by P. D. Boyer, Vol. XI, pp. 61-102. New York: Academic Press.
32. Roujeinikova, A., Levy, C. W., Rowsell, S., Sedelnikova, S., Baker, P. J., Minshull, C. A., Mistry, A., Colls, J. G., Camble, R., Stuitje, A. R., Slabas, A. R., Rafferty, J. B., Pauptit, R. A., Viner, R. & Rice, D. W. (1999). J. Mol. Biol. 294, 527-535.
33. Roujeinikova, A., Sedelnikova, S., de Boer, G. J., Stuitje, A. R., Slabas, A. R., Rafferty, J. B. & Rice, D. W. (1999). J. Biol. Chem. 274, 30811-30817.
34. Schuttelkopf, A. W. & van Aalten, D. M. F. (2004). Acta Cryst. D60, 1355-1363.
35. Tipparaju, S. K., Mulhearn, D. C., Klein, G. M., Chen, Y., Tapadar, S., Bishop, M. H., Yang, S., Chen, J., Ghassemi, M., Santarsiero, B. D., Cook, J. L., Johlfs, M., Mesecar, A. D., Johnson, M. E. & Kozikowski, A. P. (2008). Chem. Med. Chem. 3, 1250-1268.
36. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
37. Wang, F., Langley, R., Gulten, G., Dover, L. G., Besra, G. S., Jacobs, W. R. & Sacchettini, J. C. (2007). J. Exp. Med. 204, 73-78.
38. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.