Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states

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Phytases hydrolyze phytic acid to less phosphorylated myo-inositol derivatives and inorganic phosphate. A thermostable phytase is of great value in applications for improving phosphate and metal ion availability in animal feed, and thereby reducing phosphate pollution to the environment. Here, we report a new folding architecture of a six-bladed propeller for phosphatase activity revealed by the 2.1 Angstrom crystal structures of a novel, thermostable phytase determined in both the partially and fully Ca2+-loaded states. Binding of two calcium ions to high-affinity calcium binding sites results in a dramatic increase in thermostability (by as much as similar to 30 degrees C in melting temperature) by joining loop segments remote in the amino acid sequence. Binding of three additional calcium ions to low-affinity calcium binding sites at the top of the molecule turns on the catalytic activity of the enzyme by converting the highly negatively charged cleft into a favorable environment for the binding of phytate.
Publisher
NATURE AMERICA INC
Issue Date
2000-02
Language
English
Article Type
Article
Keywords

BACILLUS SP. DS11; ASPERGILLUS-FICUUM; ESCHERICHIA-COLI; G-PROTEIN; RESOLUTION; CLONING; PURIFICATION; PHOSPHATASE; SITE

Citation

NATURE STRUCTURAL BIOLOGY, v.7, no.2, pp.147 - 153

ISSN
1072-8368
URI
http://hdl.handle.net/10203/77644
Appears in Collection
BS-Journal Papers(저널논문)
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