1h6l

From Proteopedia

Revision as of 13:25, 30 October 2007

BETA-PROPELLER PHYTASE IN COMPLEX WITH PHOSPHATE AND CALCIUM IONS

Overview

BACKGROUND: Phytases hydrolyze phytic acid (myo-inositol-hexakisphosphate), to less-phosphorylated myo-inositol derivatives and inorganic phosphate., Phytases are used in animal feed to reduce phosphate pollution in the, environment. Recently, a thermostable, calcium-dependent Bacillus phytase, was identified that represents the first example of the beta propeller, fold exhibiting phosphatase activity. We sought to delineate the catalytic, mechanism and property of this enzyme. RESULTS: The crystal structure of, the enzyme in complex with inorganic phosphate reveals that two phosphates, and four calcium ions are tightly bound at the active site. Mutation of, the residues involved in the calcium chelation results in severe defects, in the enzyme's activity. One phosphate ion, chelating all ... [(full description)]

About this Structure

1H6L is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA and PO4 as [ligands]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8 and AC9. Full crystallographic information is available from [OCA].

Reference

Enzyme mechanism and catalytic property of beta propeller phytase., Shin S, Ha NC, Oh BC, Oh TK, Oh BH, Structure. 2001 Sep;9(9):851-8. PMID:11566134

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