2poo
From Proteopedia
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THERMOSTABLE PHYTASE IN FULLY CALCIUM LOADED STATE
Overview
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 Structure
2POO is a Single protein structure of sequence from Bacillus amyloliquefaciens with CA as ligand. Active as 3-phytase, with EC number 3.1.3.8 Full crystallographic information is available from OCA.
Reference
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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