PMID:10595560

Citation	Qiu, X, Janson, CA, Court, RI, Smyth, MG, Payne, DJ and Abdel-Meguid, SS (1999) Molecular basis for triclosan activity involves a flipping loop in the active site. Protein Sci. 8:2529-32
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.
Links	PubMed PMC2144207 Online version:10.1110/ps.8.11.2529
Keywords	Amino Acid Sequence; Anti-Infective Agents, Local/chemistry; Anti-Infective Agents, Local/pharmacology; Binding Sites; Crystallography, X-Ray; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); Escherichia coli/enzymology; Hydrogen Bonding; Isoleucine; Models, Molecular; Molecular Sequence Data; NAD/chemistry; NAD/metabolism; Oxidoreductases/chemistry; Oxidoreductases/metabolism; Protein Conformation; Serine; Triclosan/chemistry; Triclosan/pharmacology
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