6GIZ
PURPLE ACID PHYTASE FROM WHEAT ISOFORM B2 - SUBSTRATE COMPLEX
Summary for 6GIZ
| Entry DOI | 10.2210/pdb6giz/pdb |
| Related | 6GIT |
| Descriptor | Purple acid phosphatase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, FE (III) ION, ... (9 entities in total) |
| Functional Keywords | ec 3.1.3.26, hydrolase, purple acid phytase |
| Biological source | Triticum aestivum (Bread wheat) |
| Total number of polymer chains | 1 |
| Total formula weight | 61272.07 |
| Authors | Faba-Rodriguez, R.,Brearley, C.A.,Hemmings, A.M. (deposition date: 2018-05-15, release date: 2019-11-27, Last modification date: 2024-01-17) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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