Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states
SCIE
SCOPUS
- Title
- Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states
- Authors
- Ha, NC; Oh, BC; Shin, S; Kim, HJ; Oh, TK; Kim, YO; Choi, KY; Oh, BH
- Date Issued
- 2000-02
- Publisher
- NATURE AMERICA INC
- Abstract
- 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.
- Keywords
- BACILLUS SP. DS11; ASPERGILLUS-FICUUM; ESCHERICHIA-COLI; G-PROTEIN; RESOLUTION; CLONING; PURIFICATION; PHOSPHATASE; SITE
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/20126
- DOI
- 10.1038/72421
- ISSN
- 1072-8368
- Article Type
- Article
- Citation
- NATURE STRUCTURAL BIOLOGY, vol. 7, no. 2, page. 147 - 153, 2000-02
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