Stroud Lab
  Home / Publications / Polyketide Synthases: DEBS Thioesterase

Construct Log
Vector Log

Publications

Topics by date Topics by subject

Polyketide Synthases: DEBS Thioesterase

The Structure of a Ketoreductase Determines the Organization of the beta-Carbon Processing Enzymes of Modular Polyketide Synthases. Keatinge-Clay, A. T. and Stroud, R. M. (2006) Structure 14, 737-748.

The Structure of a Ketoreductase Determines the Organization of the b-Carbon Processing Enzymes of Modular Polyketide Synthases. Adrian T. Keatinge-Clay, and Robert M. Stroud. (2006) Structure 14, 737–748.
Download (PDF)

PKS Structure GalleryMechanism of association and reciprocal activation of two GTPases.
Shan, S. O., Stroud, R. M., Walter, P. (2004) PLoS Biol 2, e320
Download (PDF)

An antibiotic factory caught in action.
Keatinge-Clay, A. T., Maltby, D. A., Medzihradszky, K. F., Khosla, C., Stroud, R. M. (2004) Nat Struct Mol Biol 11, 888-893.
Download (PDF)

Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA: ACP transacylase.
Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.C., Miercke, L.J.W., O'Connell, J.D.3rd., Khosla, C., and Stroud, R.M. (2003) Structure (Camb) 11, 147-154.
Download PDF

Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90.
Jez, J.M., Chen, J. C., Rastelli, G., Stroud, R.M., Santi, D.V. (2003)
Chem Biol 10, 361-368.
Download PDF

Crystal structure of the priming β-ketosynthase from the R1128 polyketide biosynthetic pathway.
Pan, H., Tsai, S., Meadows, E.S., Miercke, L.J.W., Keatinge-Clay, A.T., O'Connell, J., Khosla, C., Stroud, R.M. (2002)
Structure 10: 1559-1568.
Download PDF

Insights into Channel Architecture and Substrate Specificity from Crystal Structures of Two Macrocycle Forming Thioesterases of Modular Polyketide Synthases.
Tsai, S-c., Lu, R., Khosla, C., Stroud, R.M., and Cane, D.E. (2002)
Biochemistry 41 12597-12606
Download PDF

Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthases: Versatility from a unique substrate channel.
Tsai, S.-C., Miercke, L.J.W., Krucinski, J., Gokhale, R., Chen, Julian C.-H., Foster, P.G., Cane, D.E., Khosla, C., and Stroud, R.M. (2001).
PNAS 98 26 14808-14813.
Review abstract
Download PDF

Contact Webmaster | Site by mebDESIGN