1poo: Difference between revisions

Revision as of 15:30, 21 February 2008

THERMOSTABLE PHYTASE FROM BACILLUS SP

OverviewOverview

Phytases hydrolyze phytic acid to less phosphorylated myo-inositol derivatives and inorganic phosphate. A thermostable phytase is of great value in applications for improving phosphate and metal ion availability in animal feed, and thereby reducing phosphate pollution to the environment. Here, we report a new folding architecture of a six-bladed propeller for phosphatase activity revealed by the 2.1 A crystal structures of a novel, thermostable phytase determined in both the partially and fully Ca2+-loaded states. Binding of two calcium ions to high-affinity calcium binding sites results in a dramatic increase in thermostability (by as much as approximately 30 degrees C in melting temperature) by joining loop segments remote in the amino acid sequence. Binding of three additional calcium ions to low-affinity calcium binding sites at the top of the molecule turns on the catalytic activity of the enzyme by converting the highly negatively charged cleft into a favorable environment for the binding of phytate.

About this StructureAbout this Structure

1POO is a Single protein structure of sequence from Bacillus amyloliquefaciens with as ligand. Active as 3-phytase, with EC number 3.1.3.8 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states., Ha NC, Oh BC, Shin S, Kim HJ, Oh TK, Kim YO, Choi KY, Oh BH, Nat Struct Biol. 2000 Feb;7(2):147-53. PMID:10655618

Page seeded by OCA on Thu Feb 21 14:30:52 2008

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OCA

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-[[Image:1poo.gif|left|200px]]<br /><applet load="1poo" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1poo.gif|left|200px]]<br /><applet load="1poo" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1poo, resolution 2.1&Aring;" />
 '''THERMOSTABLE PHYTASE FROM BACILLUS SP'''<br />
 ==Overview==
-Phytases hydrolyze phytic acid to less phosphorylated myo-inositol, derivatives and inorganic phosphate. A thermostable phytase is of great, value in applications for improving phosphate and metal ion availability, in animal feed, and thereby reducing phosphate pollution to the, environment. Here, we report a new folding architecture of a six-bladed, propeller for phosphatase activity revealed by the 2.1 A crystal, structures of a novel, thermostable phytase determined in both the, partially and fully Ca2+-loaded states. Binding of two calcium ions to, high-affinity calcium binding sites results in a dramatic increase in, thermostability (by as much as approximately 30 degrees C in melting, temperature) by joining loop segments remote in the amino acid sequence., Binding of three additional calcium ions to low-affinity calcium binding, sites at the top of the molecule turns on the catalytic activity of the, enzyme by converting the highly negatively charged cleft into a favorable, environment for the binding of phytate.
+Phytases hydrolyze phytic acid to less phosphorylated myo-inositol derivatives and inorganic phosphate. A thermostable phytase is of great value in applications for improving phosphate and metal ion availability in animal feed, and thereby reducing phosphate pollution to the environment. Here, we report a new folding architecture of a six-bladed propeller for phosphatase activity revealed by the 2.1 A crystal structures of a novel, thermostable phytase determined in both the partially and fully Ca2+-loaded states. Binding of two calcium ions to high-affinity calcium binding sites results in a dramatic increase in thermostability (by as much as approximately 30 degrees C in melting temperature) by joining loop segments remote in the amino acid sequence. Binding of three additional calcium ions to low-affinity calcium binding sites at the top of the molecule turns on the catalytic activity of the enzyme by converting the highly negatively charged cleft into a favorable environment for the binding of phytate.
 ==About this Structure==
-POO 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1POO OCA].
+POO 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1POO OCA].
 ==Reference==
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 [[Category: Bacillus amyloliquefaciens]]
 [[Category: Single protein]]
-[[Category: Ha, N.C.]]
+[[Category: Ha, N C.]]
-[[Category: Oh, B.H.]]
+[[Category: Oh, B H.]]
 [[Category: CA]]
 [[Category: bacillus]]
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 [[Category: thermostable]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:58:42 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:52 2008''