3k4q

Aspergillus niger Phytase in complex with myo-inositol hexakis sulfate

spinqualitylabelsall models 3k4q, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3k4q is a 2 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: IHS, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHYA_ASPNG Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic.,Oakley AJ Biochem Biophys Res Commun. 2010 Jul 9;397(4):745-9. Epub 2010 Jun 10. PMID:20541524 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phytase 3D structures

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