3K4Q

Aspergillus niger Phytase in complex with myo-inositol hexakis sulfate

Summary for 3K4Q

• Entry DOI: 10.2210/pdb3k4q/pdb
• Related: 1dkl 1dkq 1ihp 1qfx 2gfi 3k4p
• Descriptor: 3-phytase A, D-MYO-INOSITOL-HEXASULPHATE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: phytase, phya, 3-phosphotase, myo-inositol hexakis phosphate phosphohydrolase, 37288-11-2, myo-inositol hexakis sulfate, 70701-62-1, disulfide bond, glycoprotein, hydrolase, secreted
• Biological source: Aspergillus niger
• Cellular location: Secreted: P34752
• Total number of polymer chains: 2
• Total formula weight: 100868.73

Authors

Oakley, A.J. (deposition date: 2009-10-06, release date: 2010-06-30, Last modification date: 2024-10-30)

Primary citation

Oakley, A.J.
The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic
Biochem.Biophys.Res.Commun., 397:745-749, 2010

PubMed Abstract: 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.

PubMed: 20541524
DOI: 10.1016/j.bbrc.2010.06.024

Experimental method

X-RAY DIFFRACTION (2.2 Å)