PMID:9878369
| Citation |
Baldock, C, Rafferty, JB, Stuitje, AR, Slabas, AR and Rice, DW (1998) The X-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 A resolution. J. Mol. Biol. 284:1529-46 |
|---|---|
| Abstract |
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 A resolution using a combination of molecular replacement and isomorphous replacement and refined using data from 10 A to 2.1 A 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 beta-sheet flanked on each side by three alpha-helices with a further helix lying at the C terminus of the beta-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. |
| Links |
PubMed Online version:10.1006/jmbi.1998.2271 |
| Keywords |
Alcohol Dehydrogenase/chemistry; Alcohol Dehydrogenase/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Brassica/enzymology; Conserved Sequence; Crystallography, X-Ray; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); Escherichia coli/enzymology; Fatty Acid Synthetase Complex/chemistry; Fatty Acid Synthetase Complex/metabolism; Fatty Acids/metabolism; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis/enzymology; NAD/chemistry; NAD/metabolism; Nucleotides/metabolism; Oxidoreductases/chemistry; Oxidoreductases/metabolism; Protein Conformation; Protein Folding; Sequence Homology, Amino Acid; Substrate Specificity |
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