2poo
From Proteopedia
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| - | | | + | {{STRUCTURE_2poo|  PDB=2poo  |  SCENE=  }}  | 
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| '''THERMOSTABLE PHYTASE IN FULLY CALCIUM LOADED STATE''' | '''THERMOSTABLE PHYTASE IN FULLY CALCIUM LOADED STATE''' | ||
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| [[Category: Ha, N C.]] | [[Category: Ha, N C.]] | ||
| [[Category: Oh, B H.]] | [[Category: Oh, B H.]] | ||
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| - | [[Category:  | + | [[Category: Thermostable phytase]] | 
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:32:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on  | + | |
Revision as of 10:33, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 13:32:58 2008
