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Title 

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

Authors 

Nam Chul HaByung Chul OhSe Jeong ShinHyun Ju KimTae Kwang OhYoung Ok KimKwan Yong ChoiByung Ha Oh

Publisher 

Nature Publishing Group

Issue Date 

2000

Citation 

Nature Structural Biology, vol. 7, no. 2, pp. 147-153

Keywords 

amino acidcalciuminositol derivativephosphatephytasephytatephytic acidamino acid sequencecalcium bindingcrystal structure

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 ? 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 ~30°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.

ISSN 

1072-8368

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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