1ska

Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic dynamics

spinqualitylabelsall models 1ska, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ska is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Related: 1qwo, 1sk8, 1sk9, 1skb Activity: 3-phytase, with EC number 3.1.3.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PHYA_ASPFU] 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 Understanding of the atomic movements involved in an enzymatic reaction needs structural information on the active and inactive native enzyme molecules and on the enzyme-substrate, enzyme-intermediate, and enzyme-product(s) complexes. By using the X-ray crystallographic method, four crystal structures of Aspergillus fumigatus phytase were obtained at resolution higher than 1.7 A. The pH-dependent catalytic activity of A. fumigatus phytase was linked to three water molecules that may prevent the substrate from binding and thus block nucleophilic attack of the catalytic imidazole nitrogen. Comparison of various structures also identified the water molecule that attacks the phosphamide bond during the hydrolysis process, and established the hydrolysis pathway of the intermediate. Additionally, two reaction product phosphates were observed at the active site, suggesting a possible product release pathway after hydrolysis of the intermediate. These results can help explain the catalytic mechanism throughout the whole acid phosphatase family, as all key residues are conserved. Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics.,Liu Q, Huang Q, Lei XG, Hao Q Structure. 2004 Sep;12(9):1575-83. PMID:15341723 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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