β-propeller
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β-propeller
In structural biology, a beta-propeller (β-propeller) is a type of all-β protein fold, all-β protein architecture characterized by 4 to 8 highly symmetrical blade-shaped beta sheets arranged toroidally around a central axis. Together the beta-sheets form a funnel-like active site. Structure Each beta-sheet typically has four Antiparallel (biochemistry), anti-parallel beta sheet, β-strands arranged in the beta-zigzag motif. The strands are twisted so that the first and fourth strands are almost perpendicular to each other. There are five classes of beta-propellers, each arrangement being a highly symmetrical structure with 4–8 beta sheets, all of which generally form a central tunnel that yields pseudo-symmetric axes. While, the protein's official active site for ligand-binding is formed at one end of the central tunnel by loops between individual beta-strands, protein-protein interactions can occur at multiple areas around the domain. Depending on the packing and tilt of t ...
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Beta-propeller Phytase
β-propeller phytases (BPPs) are a group of enzymes (i.e. protein superfamily) with a round beta-propeller structure. BPPs are phytases, which means that they are able to remove (Hydrolysis, hydrolyze) phosphate groups from phytic acid and its phytate salts. Hydrolysis happens stepwise and usually ends in ''myo''-inositol triphosphate product which has three phosphate groups still bound to it. The actual Substrate (chemistry), substrate of BPPs is calcium phytate and in order to hydrolyze it, BPPs must have Calcium, Ca2+ ions bound to themselves. BPPs are the most widely found phytase superfamily in the environment and they are thought to have a major role in phytate-phosphorus cycling in soil and water. As their alternative name alkaline phytase suggests, BPPs work best in Base (chemistry), basic (or neutral) environment. Their pH optima is 6–9, which is unique among the phytases. Potential uses As of April 2018, BPPs are not used commercially, but they may have potential for ...
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