1dkn

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[[Image:1dkn.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 5.0 WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE==
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|PDB= 1dkn |SIZE=350|CAPTION= <scene name='initialview01'>1dkn</scene>, resolution 2.40&Aring;
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<StructureSection load='1dkn' size='340' side='right'caption='[[1dkn]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene>
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<table><tr><td colspan='2'>[[1dkn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DKN FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2]
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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]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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}}
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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=1dkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkn OCA], [https://pdbe.org/1dkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dkn RCSB], [https://www.ebi.ac.uk/pdbsum/1dkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dkn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPA_ECOLI PPA_ECOLI]
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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/dk/1dkn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1dkn 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 catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of E. coli phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of E. coli phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.
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'''CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 5.0 WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE'''
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Crystal structures of Escherichia coli phytase and its complex with phytate.,Lim D, Golovan S, Forsberg CW, Jia Z Nat Struct Biol. 2000 Feb;7(2):108-13. PMID:10655611<ref>PMID:10655611</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1dkn" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of E. coli phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of E. coli phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
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*[[Phytase 3D structures|Phytase 3D structures]]
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==About this Structure==
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== References ==
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1DKN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKN OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of Escherichia coli phytase and its complex with phytate., Lim D, Golovan S, Forsberg CW, Jia Z, Nat Struct Biol. 2000 Feb;7(2):108-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10655611 10655611]
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[[Category: Acid phosphatase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Forsberg, C W.]]
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[[Category: Forsberg CW]]
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[[Category: Golovan, S.]]
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[[Category: Golovan S]]
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[[Category: Jia, Z.]]
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[[Category: Jia Z]]
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[[Category: Lim, D.]]
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[[Category: Lim D]]
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[[Category: HG]]
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[[Category: histidine acid phosphatase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:40:01 2008''
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Current revision

CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 5.0 WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE

PDB ID 1dkn

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