1cvm

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(New page: 200px<br /><applet load="1cvm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cvm, resolution 2.40&Aring;" /> '''CADMIUM INHIBITED CR...)
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[[Image:1cvm.gif|left|200px]]<br /><applet load="1cvm" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1cvm, resolution 2.40&Aring;" />
'''CADMIUM INHIBITED CRYSTAL STRUCTURE OF PHYTASE FROM BACILLUS AMYLOLIQUEFACIENS'''<br />
'''CADMIUM INHIBITED CRYSTAL STRUCTURE OF PHYTASE FROM BACILLUS AMYLOLIQUEFACIENS'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1CVM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with CA and CD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CVM OCA].
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1CVM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVM OCA].
==Reference==
==Reference==
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[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ha, N.C.]]
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[[Category: Ha, N C.]]
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[[Category: Oh, B.H.]]
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[[Category: Oh, B H.]]
[[Category: Shin, S.]]
[[Category: Shin, S.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: thermostable bacillus phytase phytate phosphatase cadmium calcium]]
[[Category: thermostable bacillus phytase phytate phosphatase cadmium calcium]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:47:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:11 2008''

Revision as of 10:10, 21 February 2008


1cvm, resolution 2.40Å

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CADMIUM INHIBITED CRYSTAL STRUCTURE OF PHYTASE FROM BACILLUS AMYLOLIQUEFACIENS

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

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.

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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