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

Cited 123 time in scopus
Metadata Downloads
Title
Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states
Author(s)
Nam Chul Ha; Byung Chul Oh; Se Jeong Shin; Hyun Ju Kim; Tae Kwang Oh; Young Ok Kim; Kwan Yong Choi; Byung Ha Oh
Bibliographic Citation
Nature Structural & Molecular Biology, vol. 7, no. 2, pp. 147-153
Publication Year
2000
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
Publisher
Springer-Nature Pub Group
DOI
http://dx.doi.org/10.1038/72421
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.