2poo
From Proteopedia
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| |PDB= 2poo |SIZE=350|CAPTION= <scene name='initialview01'>2poo</scene>, resolution 2.050Å | |PDB= 2poo |SIZE=350|CAPTION= <scene name='initialview01'>2poo</scene>, resolution 2.050Å | ||
| |SITE=  | |SITE=  | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | 
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8]  | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span> | 
| |GENE=  | |GENE=  | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2poo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2poo OCA], [http://www.ebi.ac.uk/pdbsum/2poo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2poo RCSB]</span> | ||
| }} | }} | ||
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| [[Category: Ha, N C.]] | [[Category: Ha, N C.]] | ||
| [[Category: Oh, B H.]] | [[Category: Oh, B H.]] | ||
| - | [[Category: CA]] | ||
| [[Category: calcium loaded state]] | [[Category: calcium loaded state]] | ||
| [[Category: thermostable phytase]] | [[Category: thermostable phytase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:38:48 2008'' | 
Revision as of 01:38, 31 March 2008
 
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| , resolution 2.050Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | 3-phytase, with EC number 3.1.3.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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