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Divergent evolution of a Rossmann fold and identification of its oldest surviving ancestor
William L Duax1, Robert Huether, Vladimir Pletnev
1Hauptman-Woodward Medical Research Institute, Department of Structural Biology, University at Buffalo, 700 Ellicott St., Buffalo, NY 14203, USA. duax@hwi.buffalo.edu
Abstract:
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.
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