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1poo
From Proteopedia
(New page: 200px<br /><applet load="1poo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1poo, resolution 2.1Å" /> '''THERMOSTABLE PHYTASE ...) |
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| - | [[Image:1poo.gif|left|200px]]<br /><applet load="1poo" size=" | + | [[Image:1poo.gif|left|200px]]<br /><applet load="1poo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1poo, resolution 2.1Å" /> | caption="1poo, resolution 2.1Å" /> | ||
'''THERMOSTABLE PHYTASE FROM BACILLUS SP'''<br /> | '''THERMOSTABLE PHYTASE FROM BACILLUS SP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phytases hydrolyze phytic acid to less phosphorylated myo-inositol | + | 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== | ==About this Structure== | ||
| - | 1POO 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:// | + | 1POO 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== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ha, N | + | [[Category: Ha, N C.]] |
| - | [[Category: Oh, B | + | [[Category: Oh, B H.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: bacillus]] | [[Category: bacillus]] | ||
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[[Category: thermostable]] | [[Category: thermostable]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:52 2008'' |
Revision as of 12:30, 21 February 2008
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THERMOSTABLE PHYTASE FROM BACILLUS SP
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.
About 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.
Reference
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
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