1POO

THERMOSTABLE PHYTASE FROM BACILLUS SP

Summary for 1POO

• Entry DOI: 10.2210/pdb1poo/pdb
• Descriptor: PROTEIN (PHYTASE), CALCIUM ION (3 entities in total)
• Functional Keywords: phytasephytase, phosphatase, thermostable, bacillus, hydrolase
• Biological source: Bacillus amyloliquefaciens
• Cellular location: Secreted: O66037
• Total number of polymer chains: 1
• Total formula weight: 39088.94

Authors

Oh, B.H.,Ha, N.C. (deposition date: 1999-04-16, release date: 2000-04-19, Last modification date: 2023-12-27)

Primary citation

Ha, N.C.,Oh, B.C.,Shin, S.,Kim, H.J.,Oh, T.K.,Kim, Y.O.,Choi, K.Y.,Oh, B.H.
Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states.
Nat.Struct.Biol., 7:147-153, 2000

PubMed 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 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 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.

PubMed: 10655618
DOI: 10.1038/72421

Experimental method

X-RAY DIFFRACTION (2.1 Å)