This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1qlg
From Proteopedia
|
CRYSTAL STRUCTURE OF PHYTASE WITH MAGNESIUM FROM BACILLUS AMYLOLIQUEFACIENS
Overview
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 A 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 approximately 30 degrees C in melting, temperature) by joining loop segments remote in the amino acid sequence., Binding of three ... [(full description)]
About this Structure
1QLG is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA and MG as [ligands]. Active as [[1]], with EC number [3.1.3.8]. Full crystallographic information is available from [OCA].
Reference
Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states., Ha NC, Oh BC, Shin S, Kim HJ, Oh TK, Kim YO, Choi KY, Oh BH, Nat Struct Biol. 2000 Feb;7(2):147-53. PMID:10655618
Page seeded by OCA on Mon Oct 29 20:30:57 2007
Categories: Bacillus amyloliquefaciens | Single protein | Ha, N.C. | Oh, B.H. | Shin, S. | CA | MG | Calcium | Magnesium | Phosphatase | Phytase | Thermostable
