The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic

• Published in: Biochemical and biophysical research communications 2010-07, Vol.397 (4), p.745-749
• Main Author: Oakley, Aaron J.
• Format: Article
• Language: English
• Subjects: 3-Phytase; 6-Phytase - antagonists & inhibitors; 6-Phytase - chemistry; Aspergillus niger; Aspergillus niger - enzymology; Catalytic Domain; Crystallography, X-Ray; Inositol - analogs & derivatives; Inositol - chemistry; Michaelis complex; PhyA; Phytate; Phytic Acid - chemistry; Protein Conformation; Protein structure
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2010.06.024

► Phytases hydrolyse the phosphomonoesters of phytate. ► The structure of the A. niger 3-phytase (PhyA) has been determined with a substrate mimetic. ► The structural basis for the preference of PhyA for the 3′-phosphate of phytate is revealed. Phytases hydrolyse the phosphomonoesters of phytate ( myo-inositol-1,2,3,4,5,6-hexakis phosphate) and thus find uses in plant and animal production through the mobilisation of phosphorus from this source. The structure of partially deglycosylated Aspergillus niger PhyA is presented in apo form and in complex with the potent inhibitor myo-inositol-1,2,3,4,5,6-hexakis sulfate, which by analogy with phytate provides a snapshot of the Michaelis complex. The structure explains the enzyme’s preference for the 3′-phosphate of phytate. The apo-and inhibitor-bound forms are similar and no induced–fit mechanism operates. Furthermore the enzyme structure is apparently unaffected by the presence of glycosides on the surface. The new structures of A. niger PhyA are discussed in the context of protein engineering studies aimed at modulating pH preference and stability.