Divergent evolution of a Rossmann fold and identification of its oldest surviving ancestor.
beta-ketoacyl (acyl carrier protein) reductase (beta-k-ACPR) enzymes are essential to fatty acid synthesis in bacteria. The analyses revealed the most primitive member of the beta-k-ACPRs family was a NADP reductase where NADP was recognised by a Thr residue in the beta2alpha3 turn. Aromatic residue stacking at the dimer interface and a previously undetected conserved sequence at the C-terminus, stabilise the oligomeric assembly of these proteins. Our analysis indicates that the primordial members of the beta-k-ACPR family probably arose in the alpha-proteobacteria and are characterised by the presence of multiple open reading frames and an extreme codon and amino acid bias.
Duax
William L
WL
Hauptman-Woodward Medical Research Institute, Department of Structural Biology, University at Buffalo, 700 Ellicott St., Buffalo, NY 14203, USA. duax@hwi.buffalo.edu
Huether
Robert
R
Pletnev
Vladimir
V
Umland
Timothy C
TC
D064431:3-Oxoacyl-(Acyl-Carrier-Protein) Reductase; D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics*; D001665:Binding Sites; D019143:Evolution, Molecular; D014644:Genetic Variation; D008958:Models, Molecular; D016366:Open Reading Frames; D011487:Protein Conformation; D017510:Protein Folding
D000429:Alcohol Oxidoreductases; D064431:3-Oxoacyl-(Acyl-Carrier-Protein) Reductase