1poo: Difference between revisions

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-[[Image:1poo.gif|left|200px]]
- {{Structure
+==THERMOSTABLE PHYTASE FROM BACILLUS SP==
-|PDB= 1poo |SIZE=350|CAPTION= <scene name='initialview01'>1poo</scene>, resolution 2.1&Aring;
+<StructureSection load='1poo' size='340' side='right'caption='[[1poo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
+<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>
-|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>
+</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>
-|GENE= PHY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 Bacillus amyloliquefaciens])
+<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>
-|DOMAIN=
+<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>
-|RELATEDENTRY=
+</table>
-|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>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/PHYT_BACSD PHYT_BACSD]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1poo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''THERMOSTABLE PHYTASE FROM BACILLUS SP'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1poo" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Phytase 3D structures|Phytase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-POO is a [[Single protein]] structure of sequence from [http://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].
+__TOC__
+</StructureSection>
-==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:[http://www.ncbi.nlm.nih.gov/pubmed/10655618 10655618]
-[[Category: 3-phytase]]
 [[Category: Bacillus amyloliquefaciens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Ha, N C.]]
+[[Category: Ha NC]]
-[[Category: Oh, B H.]]
+[[Category: Oh BH]]
-[[Category: bacillus]]
-[[Category: phosphatase]]
-[[Category: phytasephytase]]
-[[Category: thermostable]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:02:26 2008''