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Crystal structures of Escherichia coli phytase and its complex with phytate.

Lim D, Golovan S, Forsberg CW, Jia Z
Nat Struct Biol 7 108-13 (2000)
Related entries: 1dkl, 1dkm, 1dkn, 1dko, 1dkp

Cited: 77 times
EuropePMC logo PMID: 10655611

Abstract

Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of E. coli phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of E. coli phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.

Articles - 1dkq mentioned but not cited (9)

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Related citations provided by authors (2)

  1. Purification, crystallization and preliminary X-ray analysis of the Escherichia coli phytase.. Jia Z, Golovan S, Ye Q, Forsberg CW Acta Crystallogr D Biol Crystallogr 54 647-9 (1998)
  2. The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase.. Dassa J, Marck C, Boquet PL J Bacteriol 172 5497-500 (1990)

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