1QLG

Crystal structure of phytase with magnesium from Bacillus amyloliquefaciens

Summary for 1QLG

• Entry DOI: 10.2210/pdb1qlg/pdb
• Descriptor: 3-PHYTASE, CALCIUM ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: phosphomonoesterase, phytase, thermostable, phosphatase, calcium, magnesium
• Biological source: BACILLUS AMYLOLIQUEFACIENS
• Cellular location: Secreted: O66037
• Total number of polymer chains: 1
• Total formula weight: 39176.64

Authors

Shin, S.,Ha, N.-C.,Oh, B.-H. (deposition date: 1999-08-31, release date: 2000-02-03, Last modification date: 2023-12-13)

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-, 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 (2.2 Å)