Structure of the Francisella tularensis enoyl-acyl carrier protein reductase (FabI) in complex with NAD+ and triclosan

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 66, Issue 11, 2010, Pages 1436-1440

  Mehboob, Shahila ^a   Truong, Kent ^a   Santarsiero, Bernard D ^a   Johnson, Michael E ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

enoyl reductases; FabI; fatty acid biosynthesis; Francisella tularensis; triclosan

Indexed keywords

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

CHEMICAL STRUCTURE; CHEMISTRY; CONFERENCE PAPER; ENZYMOLOGY; FRANCISELLA TULARENSIS; METABOLISM; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; ENOYL-(ACYL-CARRIER-PROTEIN) REDUCTASE (NADH); ENZYME INHIBITORS; FRANCISELLA TULARENSIS; MODELS, MOLECULAR; NAD; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN; TRICLOSAN;

BACTERIA (MICROORGANISMS); FRANCISELLA TULARENSIS;

EID: 78149327152     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309110039862     Document Type: Conference Paper

References (17)

1. Adams, P. D. et al. (2010). Acta Cryst. D66, 213-221.
2. 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.
3. Bergler, H., Fuchsbichler, S., Hogenauer, G. & Turnowsky, F. (1996). Eur. J. Biochem. 242, 689-694.
4. 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.
5. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
6. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
7. Kabsch, W. (2010). Acta Cryst. D66, 125-132.
8. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
9. 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.
10. 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.
11. Lu, H. & Tonge, P. J. (2008). Acc. Chem. Res. 41, 11-20.
12. 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.
13. Parikh, S., Moynihan, D. P., Xiao, G. & Tonge, P. J. (1999). Biochemistry, 38, 13623-13634.
14. Priyadarshi, A., Kim, E. E. & Hwang, K. Y. (2010). Proteins, 78, 480-486.
15. Stewart, M. J., Parikh, S., Xiao, G., Tonge, P. J. & Kisker, C. (1999). J. Mol. Biol. 290, 859-865.
16. Vagin, A. A., Steiner, R. A., Lebedev, A. A., Potterton, L., McNicholas, S., Long, F. & Murshudov, G. N. (2004). Acta Cryst. D60, 2184-2195.
17. Wen, L., Chmielowski, J. N., Bohn, K. C., Huang, J.-K., Timsina, Y. N., Kodali, P. & Pathak, A. K. (2009). Protein Expr. Purif. 65, 83-91.