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Plants, lower eukaryotes, bacteria, and archaebacteria synthesise L-histidine (His) in a similar, multistep pathway that is absent in mammals. This makes the His biosynthetic route a promising target for herbicides, antifungal agents, and antibiotics. The last enzyme of the pathway, bifunctional L-histidinol dehydrogenase (HDH, EC 1.1.1.23), catalyses two oxidation reactions: from L-histidinol (HOL) to L-histidinaldehyde and from L-histidinaldehyde to His. Over the course of the reaction, HDH utilises two molecules of NAD +  as the hydride acceptor. The object of this study was the HDH enzyme from the model legume plant,  Medicago truncatula  ( Mt HDH). Three crystal structures complexed with imidazole, HOL, and His with NAD +  provided in-depth insights into the enzyme architecture, its active site, and the cofactor binding mode. The overall structure of  Mt HDH is similar to the two bacterial orthologues whose three-dimensional structures have been determined. The three snapshots, with the  Mt HDH enzyme captured in different states, visualise structural rearrangements that allow for NAD +  binding for the first time. Furthermore, the  Mt HDH complex with His and NAD +  displays the cofactor molecule situated in a way that would allow for a hydride transfer.

scientific reports

Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD+ Binding and the Cofactor Positioned to Accept a Hydride