Molecular basis for triclosan activity involves a flipping loop in the active site.
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Qiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS
Molecular basis for triclosan activity involves a flipping loop in the active site.
Protein Sci. 1999 Nov;8(11):2529-32.
- PubMed ID
- 10595560 [ View in PubMed]
- Abstract
The crystal structure of the Escherichia coli enoyl reductase-NAD+-triclosan complex has been determined at 2.5 A resolution. The Ile192-Ser198 loop is either disordered or in an open conformation in the previously reported structures of the enzyme. This loop adopts a closed conformation in our structure, forming van der Waals interactions with the inhibitor and hydrogen bonds with the bound NAD+ cofactor. The opening and closing of this flipping loop is likely an important factor in substrate or ligand recognition. The closed conformation of the loop appears to be a critical feature for the enhanced binding potency of triclosan, and a key component in future structure-based inhibitor design.