7B81

Crystal structure of Azotobacter vinelandii L-rhamnose 1-dehydrogenase (NAD bound-form)

7B81 の概要

• エントリーDOI: 10.2210/pdb7b81/pdb
• 分子名称: Short-chain dehydrogenase/reductase SDR, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: l-rhanose metabolism, nadp-dependent dehydrogenase, sdr protein family, oxidoreductase
• 由来する生物種: Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56768.11

構造登録者

Yoshiwara, K.,Watanabe, Y.,Watanabe, S. (登録日: 2020-12-12, 公開日: 2021-02-03, 最終更新日: 2024-05-01)

主引用文献

Yoshiwara, K.,Watanabe, S.,Watanabe, Y.
Crystal structure of l-rhamnose 1-dehydrogenase involved in the nonphosphorylative pathway of l-rhamnose metabolism in bacteria.
Febs Lett., 595:637-646, 2021

PubMed Abstract: Several microorganisms can utilize l-rhamnose as a carbon and energy source through the nonphosphorylative metabolic pathway, in which l-rhamnose 1-dehydrogenase (RhaDH) catalyzes the NAD(P) -dependent oxidization of l-rhamnose to l-rhamnono-1,4-lactone. We herein investigated the crystal structures of RhaDH from Azotobacter vinelandii in ligand-free, NAD -bound, NADP -bound, and l-rhamnose- and NAD -bound forms at 1.9, 2.1, 2.4, and 1.6 Å resolution, respectively. The significant interactions with the 2'-phosphate group of NADP , but not the 2'-hydroxyl group of NAD , were consistent with a preference for NADP over NAD . The C5-OH and C6-methyl groups of l-rhamnose were recognized by specific residues of RhaDH through hydrogen bonds and hydrophobic contact, respectively, which contribute to the different substrate specificities from other aldose 1-dehydrogenases in the short-chain dehydrogenase/reductase superfamily.

PubMed: 33482017
DOI: 10.1002/1873-3468.14046

実験手法

X-RAY DIFFRACTION (2.092 Å)