Fig. 3: Comparison of the structure of AdhE in its extended conformation with monofunctional ADH and AlDH enzymes. | Nature Communications

Fig. 3: Comparison of the structure of AdhE in its extended conformation with monofunctional ADH and AlDH enzymes.

From: Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation

Fig. 3

a The structures of the monofunctional enzyme propionaldehyde dehydrogenase from R. palustris (left) and AdhE AlDH domain (right) are compared. The monomers share the same overall fold. The root-mean-square deviation of atomic positions (RMSD) between the two structures is indicated in the figure. Both enzymes assemble as dimers, which are superimposable with each other. b The structures of the monofunctional enzyme lactaldehyde : 1,2-propanediol oxidoreductase from E. coli and AdhE ADH domain are compared. The monomers share the same overall fold. The RMSD between the two structures is indicated in the figure. Both enzymes assemble as dimers, which are superimposable with each other. c Localization and conservation of three loops specific to AdhE. These loops are not present in the monofunctional enzymes but are conserved in AdhE homologs.

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