1dkl

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[[Image:1dkl.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 4.5 (NO LIGAND BOUND)==
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|PDB= 1dkl |SIZE=350|CAPTION= <scene name='initialview01'>1dkl</scene>, resolution 2.30&Aring;
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<StructureSection load='1dkl' size='340' side='right'caption='[[1dkl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1dkl]] is a 2 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=1DKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DKL 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]] 2.3&#8491;</td></tr>
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|GENE=
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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=1dkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkl OCA], [https://pdbe.org/1dkl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dkl RCSB], [https://www.ebi.ac.uk/pdbsum/1dkl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dkl ProSAT]</span></td></tr>
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}}
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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/1dkl_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=1dkl 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 4.5 (NO LIGAND BOUND)'''
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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 1dkl" 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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*[[Art:Molecular Sculpture|Art:Molecular Sculpture]]
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==About this Structure==
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*[[Phytase 3D structures|Phytase 3D structures]]
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1DKL 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=1DKL OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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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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</StructureSection>
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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: histidine acid phosphatase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:39:55 2008''
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Current revision

CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 4.5 (NO LIGAND BOUND)

PDB ID 1dkl

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