5VLC

Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol

5VLC の概要

• エントリーDOI: 10.2210/pdb5vlc/pdb
• 関連するPDBエントリー: 5VLB 5VLD
• 分子名称: Histidinol dehydrogenase, chloroplastic, L-histidinol, ZINC ION, ... (4 entities in total)
• 機能のキーワード: histidine biosynthesis, zn2+ binding protein, nad binding protein, plant protein, oxidoreductase
• 由来する生物種: Medicago truncatula (Barrel medic)
• 細胞内の位置: Plastid, chloroplast : G7IKX3
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 290407.91

構造登録者

Ruszkowski, M.,Dauter, Z. (登録日: 2017-04-25, 公開日: 2017-09-20, 最終更新日: 2023-11-15)

主引用文献

Ruszkowski, M.,Dauter, Z.
Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD(+) Binding and the Cofactor Positioned to Accept a Hydride.
Sci Rep, 7:10476-10476, 2017

PubMed Abstract: 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 (MtHDH). 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 MtHDH is similar to the two bacterial orthologues whose three-dimensional structures have been determined. The three snapshots, with the MtHDH enzyme captured in different states, visualise structural rearrangements that allow for NAD binding for the first time. Furthermore, the MtHDH complex with His and NAD displays the cofactor molecule situated in a way that would allow for a hydride transfer.

PubMed: 28874718
DOI: 10.1038/s41598-017-10859-0

実験手法

X-RAY DIFFRACTION (1.97 Å)