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1poo

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(New page: 200px<br /><applet load="1poo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1poo, resolution 2.1&Aring;" /> '''THERMOSTABLE PHYTASE ...)
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[[Image:1poo.gif|left|200px]]<br /><applet load="1poo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1poo, resolution 2.1&Aring;" />
 
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'''THERMOSTABLE PHYTASE FROM BACILLUS SP'''<br />
 
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==Overview==
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==THERMOSTABLE PHYTASE FROM BACILLUS SP==
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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.
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<StructureSection load='1poo' size='340' side='right'caption='[[1poo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1poo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1POO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1poo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poo OCA], [https://pdbe.org/1poo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1poo RCSB], [https://www.ebi.ac.uk/pdbsum/1poo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1poo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHYT_BACSD PHYT_BACSD]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1poo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1poo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:10655618</ref>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1POO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10655618 10655618]
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</div>
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[[Category: 3-phytase]]
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<div class="pdbe-citations 1poo" style="background-color:#fffaf0;"></div>
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[[Category: Bacillus amyloliquefaciens]]
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[[Category: Single protein]]
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[[Category: Ha, N.C.]]
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[[Category: Oh, B.H.]]
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[[Category: CA]]
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[[Category: bacillus]]
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[[Category: phosphatase]]
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[[Category: phytasephytase]]
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[[Category: thermostable]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:58:42 2007''
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==See Also==
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*[[Phytase 3D structures|Phytase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus amyloliquefaciens]]
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[[Category: Large Structures]]
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[[Category: Ha NC]]
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[[Category: Oh BH]]

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THERMOSTABLE PHYTASE FROM BACILLUS SP

PDB ID 1poo

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