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X-ray Structural Analysis of Plasmodium falciparum Enoyl Acyl Carrier Protein Reductase as a Pathway toward the Optimization of Triclosan Antimalarial Efficacy

✍ Scribed by Freundlich, J. S.; Wang, F.; Tsai, H.-C.; Kuo, M.; Shieh, H.-M.; Anderson, J. W.; Nkrumah, L. J.; Valderramos, J.-C.; Yu, M.; Kumar, T. R. S.; Valderramos, S. G.; Jacobs, W. R.; Schiehser, G. A.; Jacobus, D. P.; Fidock, D. A.; Sacchettini, J. C.

Book ID: 118155090
Publisher: The American Society for Biochemistry and Molecular Biology
Year: 2007
Tongue: English
Weight: 479 KB
Volume: 282
Category: Article
ISSN: 0021-9258
DOI: 10.1074/jbc.m701813200

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X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition

✍ Koustav Maity; Saligram Prabhakar Bhargav; Banumathi Sankaran; Namita Surolia; A 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 378 KB

## Abstract Triclosan, a well‐known inhibitor of Enoyl Acyl Carrier Protein Reductase (ENR) from several pathogenic organisms, is a promising lead compound to design effective drugs. We have solved the X‐ray crystal structures of __Plasmodium falciparum__ ENR in complex with triclosan variants havi