1cvm: Difference between revisions
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|PDB= 1cvm |SIZE=350|CAPTION= <scene name='initialview01'>1cvm</scene>, resolution 2.40Å | |PDB= 1cvm |SIZE=350|CAPTION= <scene name='initialview01'>1cvm</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</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=[[1poo|1POO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvm OCA], [http://www.ebi.ac.uk/pdbsum/1cvm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cvm RCSB]</span> | |||
}} | }} | ||
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[[Category: Oh, B H.]] | [[Category: Oh, B H.]] | ||
[[Category: Shin, S.]] | [[Category: Shin, S.]] | ||
[[Category: thermostable bacillus phytase phytate phosphatase cadmium calcium]] | [[Category: thermostable bacillus phytase phytate phosphatase cadmium calcium]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:29:28 2008'' | ||
Revision as of 19:29, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | 3-phytase, with EC number 3.1.3.8 | ||||||
| Related: | 1POO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CADMIUM INHIBITED CRYSTAL STRUCTURE OF PHYTASE FROM BACILLUS AMYLOLIQUEFACIENS
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. 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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