7S5F

Crystal structure of mannose-6-phosphate reductase from celery (Apium graveolens) leaves with NADP+ and mannonic acid bound

7S5F の概要

• エントリーDOI: 10.2210/pdb7s5f/pdb
• 分子名称: Manose-6-phosphate reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, D-MANNONIC ACID, ... (4 entities in total)
• 機能のキーワード: aldo/keto reductase superfamily, aldose-6-phosphate reductase, apium graveolens, celery, mannose-6-phosphate reductase, peach, prunus persica, oxidoreductase
• 由来する生物種: Apium graveolens (Celery)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 144679.94

構造登録者

Zheng, Y.,Bhayani, J.A.,Romina, I.M.,Hartman, M.D.,Cereijo, A.E.,Ballicora, M.A.,Iglesias, A.A.,Figueroa, C.M.,Liu, D. (登録日: 2021-09-10, 公開日: 2022-03-16, 最終更新日: 2023-10-18)

主引用文献

Minen, R.I.,Bhayani, J.A.,Hartman, M.D.,Cereijo, A.E.,Zheng, Y.,Ballicora, M.A.,Iglesias, A.A.,Liu, D.,Figueroa, C.M.
Structural Determinants of Sugar Alcohol Biosynthesis in Plants: The Crystal Structures of Mannose-6-Phosphate and Aldose-6-Phosphate Reductases.
Plant Cell.Physiol., 63:658-670, 2022

PubMed Abstract: Sugar alcohols are major photosynthetic products in plant species from the Apiaceae and Plantaginaceae families. Mannose-6-phosphate reductase (Man6PRase) and aldose-6-phosphate reductase (Ald6PRase) are key enzymes for synthesizing mannitol and glucitol in celery (Apium graveolens) and peach (Prunus persica), respectively. In this work, we report the first crystal structures of dimeric plant aldo/keto reductases (AKRs), celery Man6PRase (solved in the presence of mannonic acid and NADP+) and peach Ald6PRase (obtained in the apo form). Both structures displayed the typical TIM barrel folding commonly observed in proteins from the AKR superfamily. Analysis of the Man6PRase holo form showed that residues putatively involved in the catalytic mechanism are located close to the nicotinamide ring of NADP+, where the hydride transfer to the sugar phosphate should take place. Additionally, we found that Lys48 is important for the binding of the sugar phosphate. Interestingly, the Man6PRase K48A mutant had a lower catalytic efficiency with mannose-6-phosphate but a higher catalytic efficiency with mannose than the wild type. Overall, our work sheds light on the structure-function relationships of important enzymes to synthesize sugar alcohols in plants.

PubMed: 35243499
DOI: 10.1093/pcp/pcac029

実験手法

X-RAY DIFFRACTION (1.72 Å)