Heavy Metal-Mediated Crystallization of Escherichia Coli Phytase and Analysis of Bridging Interactions

Authors: Lim D.; Jia Z.

Source: Protein and Peptide Letters, Volume 9, Number 4, August 2002 , pp. 359-365(7)

Publisher: Bentham Science Publishers

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Abstract:

Escherichia coli phytase is a phosphatase that catalyzes the hydrolysis of phytic acid into inorganic phosphate and myo-inositol. Two crystal forms of this enzyme were obtained in the presence of heavy metals.Crystal forms I and II were obtained with the heavy atoms CdCl2 and HgCl2 and diffracted to 1.5 Å and 2.25 Å resolution, respectively. Hg2+ and Cd2+ both acted as molecular bridge(s), linking and stabilizing E. coli phytase in the unit cell, and played a crucial role in the crystallization of phytase by bridging neighbouring symmetry related molecules.

Keywords: Heavy Metal; Escherichia Coli; myo-inositol

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023408634

Publication date: 2002-08-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.