1cvm
CADMIUM INHIBITED CRYSTAL STRUCTURE OF PHYTASE FROM BACILLUS AMYLOLIQUEFACIENS
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OverviewOverview
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 M MES (pH 6.5). Native diffraction data to 2.0 A 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 A 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.
About this StructureAbout this Structure
1CVM is a Single protein structure of sequence from Bacillus amyloliquefaciens with and as ligands. Active as 3-phytase, with EC number 3.1.3.8 Full crystallographic information is available from OCA.
ReferenceReference
Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain., Ha NC, Kim YO, Oh TK, Oh BH, Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):691-3. PMID:10089471
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