6git

PURPLE ACID PHYTASE FROM WHEAT ISOFORM B2 - PRODUCT COMPLEX

spinqualitylabelsall models 6git, resolution 1.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6git is a 1 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.418Å Ligands: 1PE, EDO, FE, NAG, PEG, PGE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F6MIW5_WHEAT Publication Abstract from PubMed 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 in planta. Structure of a cereal purple acid phytase provides new insights to phytate degradation in plants.,Faba-Rodriguez R, Gu Y, Salmon M, Dionisio G, Brinch-Pedersen H, Brearley CA, Hemmings AM Plant Commun. 2022 Feb 19;3(2):100305. doi: 10.1016/j.xplc.2022.100305. , eCollection 2022 Mar 14. PMID:35529950 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acid phosphatase 3D structures Phytase 3D structures

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