1C14

CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX

Summary for 1C14

• Entry DOI: 10.2210/pdb1c14/pdb
• Descriptor: ENOYL REDUCTASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, TRICLOSAN, ... (4 entities in total)
• Functional Keywords: triclosan, fabi, enoyl reductase, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 57691.79

Authors

Qiu, X.,Janson, C.,Court, R.,Smyth, M.,Payne, D.,Abdel-Meguid, S. (deposition date: 1999-07-20, release date: 2000-07-20, Last modification date: 2024-02-07)

Primary citation

Qiu, X.,Janson, C.A.,Court, R.I.,Smyth, M.G.,Payne, D.J.,Abdel-Meguid, S.S.
Molecular basis for triclosan activity involves a flipping loop in the active site.
Protein Sci., 8:2529-2532, 1999

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.

PubMed: 10595560

Experimental method

X-RAY DIFFRACTION (2 Å)