Fig. 4: A continuous channel between the ADH and AlDH active sites.
a A conserved channel crosses the monofunctional propionaldehyde dehydrogenase from R. palustris (left panels). This channel is conserved in the AlDH domain in AdhE (right panel). Top, cut-out slice through the AlDH domain of the bottom, surface representation of the AlDH domain showing the substrate entrance/exit channel (opposite of the NAD-binding channel). b A conserved channel crosses the monofunctional lactaldehyde : 1,2-propanediol oxidoreductase from E. coli (left panels). This channel is conserved in the ADH domain in AdhE (right panel). Top, cut-out slice through the ADH domain of the bottom, surface representation of the ADH domain showing the substrate entrance/exit channel (opposite of the NAD-binding channel). c Surface representation of ADHα (in light blue) and AlDHβ (in blue). The loops 2 and 3 from ADHα are colored in red. d A channel connects directly the active sites of ADHα (in light blue) and AlDHβ (in blue). The domains are represented as transparent surfaces and ribbons with the same color code than above. A surface representation of channel is colored in yellow. Surface representations of NAD+ molecules bound to ADH and AlDH domains are colored in green.
