1poo

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[[Image:1poo.gif|left|200px]]
[[Image:1poo.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1poo |SIZE=350|CAPTION= <scene name='initialview01'>1poo</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1poo", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= PHY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 Bacillus amyloliquefaciens])
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-->
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|DOMAIN=
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{{STRUCTURE_1poo| PDB=1poo | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1poo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poo OCA], [http://www.ebi.ac.uk/pdbsum/1poo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1poo RCSB]</span>
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}}
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'''THERMOSTABLE PHYTASE FROM BACILLUS SP'''
'''THERMOSTABLE PHYTASE FROM BACILLUS SP'''
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[[Category: Ha, N C.]]
[[Category: Ha, N C.]]
[[Category: Oh, B H.]]
[[Category: Oh, B H.]]
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[[Category: bacillus]]
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[[Category: Bacillus]]
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[[Category: phosphatase]]
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[[Category: Phosphatase]]
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[[Category: phytasephytase]]
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[[Category: Phytasephytase]]
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[[Category: thermostable]]
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[[Category: Thermostable]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:18:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:02:26 2008''
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Revision as of 02:18, 3 May 2008

Template:STRUCTURE 1poo

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. 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 Page seeded by OCA on Sat May 3 05:18:49 2008

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