6JNK

Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (NADP-bound form)

6JNK の概要

• エントリーDOI: 10.2210/pdb6jnk/pdb
• 分子名称: L-arabinose 1-dehydrogenase (NAD(P)(+)), NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: l-arabinose metabolism, nadp-dependent dehydrogenase, gfo/idh/moca protein family, oxidoreductase
• 由来する生物種: Azospirillum brasilense
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 138419.54

構造登録者

Watanabe, Y.,Iga, C.,Watanabe, S. (登録日: 2019-03-16, 公開日: 2019-05-15, 最終更新日: 2024-03-27)

主引用文献

Watanabe, Y.,Iga, C.,Watanabe, Y.,Watanabe, S.
Structural insights into the catalytic and substrate recognition mechanisms of bacterial l-arabinose 1-dehydrogenase.
Febs Lett., 593:1257-1266, 2019

PubMed Abstract: In Azospirillum brasilense, a gram-negative nitrogen-fixing bacterium, l-arabinose is converted to α-ketoglutarate through a nonphosphorylative metabolic pathway. In the first step in the pathway, l-arabinose is oxidized to l-arabino-γ-lactone by NAD(P)-dependent l-arabinose 1-dehydrogenase (AraDH) belonging to the glucose-fructose oxidoreductase/inositol dehydrogenase/rhizopine catabolism protein (Gfo/Idh/MocA) family. Here, we determined the crystal structures of apo- and NADP-bound AraDH at 1.5 and 2.2 Å resolutions, respectively. A docking model of l-arabinose and NADP-bound AraDH and structure-based mutational analyses suggest that Lys91 or Asp169 serves as a catalytic base and that Glu147, His153, and Asn173 are responsible for substrate recognition. In particular, Asn173 may play a role in the discrimination between l-arabinose and d-xylose, the C4 epimer of l-arabinose.

PubMed: 31058311
DOI: 10.1002/1873-3468.13424

実験手法

X-RAY DIFFRACTION (2.2 Å)