The X-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 Å resolution

Clair Baldock, John B. Rafferty, Antoine R. Stuitje, Antoni R. Slabas, David W. Rice

    Research output: Contribution to journalArticlepeer-review


    Enoyl acyl carrier protein reductase catalyses the last reductive step of fatty acid biosynthesis, reducing an enoyl acyl carrier protein to an acyl-acyl carrier protein with NAD(P)H as the cofactor. The crystal structure of enoyl reductase (ENR) from Escherichia coli has been determined to 2.1 Å resolution using a combination of molecular replacement and isomorphous replacement and refined using data from 10 Å to 2.1 Å to an R-factor of 0.16. The final model consists of the four subunits of the tetramer, wherein each subunit is composed of 247 of the expected 262 residues, and a NAD+ cofactor for each subunit of the tetramer contained in the asymmetric unit plus a total of 327 solvent molecules. There are ten disordered residues per subunit which form a loop near the nucleotide binding site which may become ordered upon substrate binding. Each monomer is composed of a seven-stranded parallel β-sheet flanked on each side by three α-helices with a further helix lying at the C terminus of the β-sheet. This fold is highly reminiscent of the Rossmann fold, found in many NAD(P)H-dependent enzymes. Analysis of the sequence and structure of ENR and comparisons with the family of short-chain alcohol dehydrogenases, identify a conserved tyrosine and lysine residue as important for catalytic activity. Modelling studies suggest that a region of the protein surface that contains a number of strongly conserved hydrophobic residues and lies adjacent to the nicotinamide ring, forms the binding site for the fatty acid substrate.
    Original languageEnglish
    Pages (from-to)1529-1546
    Number of pages17
    JournalJournal of molecular biology
    Issue number5
    Publication statusPublished - 18 Dec 1998


    • Enoyl reductase
    • Fatty acid biosynthesis
    • NAD
    • Structure comparison
    • Tuberculosis


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