Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens

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Title
Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens
Author(s)
Nam Chul Ha; Young Ok Kim; Tae Kwang Oh; Byung Ha Oh
Bibliographic Citation
Acta Crystallographica Section D-Biological Crystallography, vol. 55, pp. 691-693
Publication Year
1999
Abstract
A novel bacterial phytase from a Bacillus amyloliquefaciens strain was crystallized using the hanging-drop vapour-diffusion method. The amino-acid sequence of the enzyme does not show any homology to those of other known phytases or phosphatases, with the exception of a phytase from Bacillus subtilis. The enzyme exhibits a thermal stability which is strongly dependent on calcium ions. High-quality single crystals of the enzyme in the absence of calcium ions were obtained using a precipitant solution containing 20% 2-methyl-2,4-pentanediol and 0.1 MMES (pH 6.5). Native diffraction data to 2.0 ? resolution were obtained from a flash-frozen crystal at 110 K using a rotating-anode X-ray source. The crystals belong to space group P212121 with unit-cell dimensions a = 50.4, b = 64.1, c = 104.2 ? and contain one monomer per asymmetric unit. Structure determination using heavy-atom derivative crystals is in progress, along with an effort to crystallize the calcium ion bound form of the enzyme.
ISSN
0907-4449
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S0907444998015285
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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