6GIT
PURPLE ACID PHYTASE FROM WHEAT ISOFORM B2 - PRODUCT COMPLEX
6GIT の概要
エントリーDOI | 10.2210/pdb6git/pdb |
分子名称 | Purple acid phosphatase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, FE (III) ION, ... (10 entities in total) |
機能のキーワード | ec 3.1.3.26, hydrolase, purple acid phytase |
由来する生物種 | Triticum aestivum (Bread wheat) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 61416.40 |
構造登録者 | Faba-Rodriguez, R.,Brearley, C.A.,Hemmings, A.M. (登録日: 2018-05-15, 公開日: 2019-11-27, 最終更新日: 2024-10-09) |
主引用文献 | Faba-Rodriguez, R.,Gu, Y.,Salmon, M.,Dionisio, G.,Brinch-Pedersen, H.,Brearley, C.A.,Hemmings, A.M. Structure of a cereal purple acid phytase provides new insights to phytate degradation in plants. Plant Commun., 3:100305-100305, 2022 Cited by PubMed Abstract: Grain phytate, a mixed metal ion salt of inositol hexakisphosphate, accounts for 60%-80% of stored phosphorus in plants and is a potent antinutrient of non-ruminant animals including humans. Through neofunctionalization of purple acid phytases (PAPhy), some cereals such as wheat and rye have acquired particularly high mature grain phytase activity. As PAPhy activity supplies phosphate, liberates metal ions necessary for seedling emergence, and obviates antinutrient effects of phytate, its manipulation and control are targeted crop traits. Here we show the X-ray crystal structure of the b2 isoform of wheat PAPhy induced during germination. This high-resolution crystal structure suggests a model for phytate recognition that, validated by molecular dynamics simulations, implicates elements of two sequence inserts (termed PAPhy motifs) relative to a canonical metallophosphoesterase (MPE) domain in forming phytate-specific substrate specificity pockets. These motifs are well conserved in PAPhys from monocot cereals, enzymes which are characterized by high specificity for phytate. Tested by mutagenesis, residues His229 in PAPhy motif 4 and Lys410 in the MPE domain, both conserved in PAPhys, are found to strongly influence phytase activity. These results explain the observed phytase activity of cereal PAPhys and open the way to the rational engineering of phytase activity . PubMed: 35529950DOI: 10.1016/j.xplc.2022.100305 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.418 Å) |
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