1CVM

CADMIUM INHIBITED CRYSTAL STRUCTURE OF PHYTASE FROM BACILLUS AMYLOLIQUEFACIENS

Summary for 1CVM

• Entry DOI: 10.2210/pdb1cvm/pdb
• Related: 1POO
• Descriptor: PHYTASE, CALCIUM ION, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: thermostable bacillus phytase phytate phosphatase cadmium calcium, hydrolase
• Biological source: Bacillus amyloliquefaciens
• Cellular location: Secreted: O66037
• Total number of polymer chains: 1
• Total formula weight: 39503.85

Authors

Shin, S.,Ha, N.-C.,Oh, B.-H. (deposition date: 1999-08-24, release date: 2000-02-24, Last modification date: 2024-02-07)

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 (2.4 Å)