Introduction
Pytate is a small compound responsible for storing more than 80% of the total phosporus in cereals and legumes. Many commercially important animals, such as pigs, poultry, and fish cannot metabolize phytate, and thus excrete a lot of phosphorus, creating environmental problems. Addition of a phytase to animal feed helps alleviate the problem. Unfortunately, animal feed must be processed at 58 deg. C, so only a highly stable enzyme will do the job. Such a protein has been isolated from Bacillus amyloliquefaciens, prompting the Ha et al the crystallize it to find out what makes it so stable.
Basic Structure
This protein represents a novel scaffold for phytase activity. It is predominantly a beta structure. Ha et al liken its appearance to a propeller with six blades. Each blade is composed of four or five curved beta sheets, and the topology of each blade is identical. One of the features of the protein that may contribute to its stability is a structural element that has been termed double clasp. The N-terminal segment of the protein forms part of the two C-terminal blades. In this manner it is proposed to stabilize the circular arrangent of blade domains.