High-resolution structures of Thermus thermophilus enoyl-acyl carrier protein reductase in the apo form, in complex with NAD⁺ and in complex with NAD⁺ and triclosan

T. thermophilus enoyl-acyl carrier protein reductase was crystallized in the apo form, with NAD⁺ bound and with NAD⁺ and the inhibitor triclosan bound. The structures were solved by molecular replacement and refined at 1.50, 1.86 and 1.90 Å resolution, respectively. The structures are described, analysed and compared with those of enoyl-acyl carrier protein reductases from other species.