1e1a

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[[Image:1e1a.jpg|left|200px]]
 
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==Crystal structure of DFPase from Loligo vulgaris==
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The line below this paragraph, containing "STRUCTURE_1e1a", creates the "Structure Box" on the page.
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<StructureSection load='1e1a' size='340' side='right'caption='[[1e1a]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1e1a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Loligo_vulgaris Loligo vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E1A 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]] 1.8&#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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{{STRUCTURE_1e1a| PDB=1e1a | SCENE= }}
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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=1e1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e1a OCA], [https://pdbe.org/1e1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e1a RCSB], [https://www.ebi.ac.uk/pdbsum/1e1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e1a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DFPA_LOLVU DFPA_LOLVU] Biological function and substrate unknown. However, it is capable of acting on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including nerve gases).<ref>PMID:15966726</ref>
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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/e1/1e1a_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=1e1a 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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BACKGROUND: Phosphotriesterases (PTE) are enzymes capable of detoxifying organophosphate-based chemical warfare agents by hydrolysis. One subclass of these enzymes comprises the family of diisopropylfluorophosphatases (DFPases). The DFPase reported here was originally isolated from squid head ganglion of Loligo vulgaris and can be characterized as squid-type DFPase. It is capable of hydrolyzing the organophosphates diisopropylfluorophosphate, soman, sarin, tabun, and cyclosarin. RESULTS: Crystals were grown of both the native and the selenomethionine-labeled enzyme. The X-ray crystal structure of the DFPase from Loligo vulgaris has been solved by MAD phasing and refined to a crystallographic R value of 17.6% at a final resolution of 1.8 A. Using site-directed mutagenesis, we have structurally and functionally characterized essential residues in the active site of the enzyme. CONCLUSIONS: The crystal structure of the DFPase from Loligo vulgaris is the first example of a structural characterization of a squid-type DFPase and the second crystal structure of a PTE determined to date. Therefore, it may serve as a structural model for squid-type DFPases in general. The overall structure of this protein represents a six-fold beta propeller with two calcium ions bound in a central water-filled tunnel. The consensus motif found in the blades of this beta propeller has not yet been observed in other beta propeller structures. Based on the results obtained from mutants of active-site residues, a mechanistic model for the DFP hydrolysis has been developed.
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'''CRYSTAL STRUCTURE OF DFPASE FROM LOLIGO VULGARIS'''
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Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris.,Scharff EI, Koepke J, Fritzsch G, Lucke C, Ruterjans H Structure. 2001 Jun;9(6):493-502. PMID:11435114<ref>PMID:11435114</ref>
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==Overview==
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BACKGROUND: Phosphotriesterases (PTE) are enzymes capable of detoxifying organophosphate-based chemical warfare agents by hydrolysis. One subclass of these enzymes comprises the family of diisopropylfluorophosphatases (DFPases). The DFPase reported here was originally isolated from squid head ganglion of Loligo vulgaris and can be characterized as squid-type DFPase. It is capable of hydrolyzing the organophosphates diisopropylfluorophosphate, soman, sarin, tabun, and cyclosarin. RESULTS: Crystals were grown of both the native and the selenomethionine-labeled enzyme. The X-ray crystal structure of the DFPase from Loligo vulgaris has been solved by MAD phasing and refined to a crystallographic R value of 17.6% at a final resolution of 1.8 A. Using site-directed mutagenesis, we have structurally and functionally characterized essential residues in the active site of the enzyme. CONCLUSIONS: The crystal structure of the DFPase from Loligo vulgaris is the first example of a structural characterization of a squid-type DFPase and the second crystal structure of a PTE determined to date. Therefore, it may serve as a structural model for squid-type DFPases in general. The overall structure of this protein represents a six-fold beta propeller with two calcium ions bound in a central water-filled tunnel. The consensus motif found in the blades of this beta propeller has not yet been observed in other beta propeller structures. Based on the results obtained from mutants of active-site residues, a mechanistic model for the DFP hydrolysis has been developed.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1E1A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Loligo_vulgaris Loligo vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E1A OCA].
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</div>
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<div class="pdbe-citations 1e1a" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris., Scharff EI, Koepke J, Fritzsch G, Lucke C, Ruterjans H, Structure. 2001 Jun;9(6):493-502. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11435114 11435114]
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*[[Serum Paraoxonase|Serum Paraoxonase]]
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[[Category: Diisopropyl-fluorophosphatase]]
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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: Large Structures]]
[[Category: Loligo vulgaris]]
[[Category: Loligo vulgaris]]
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[[Category: Single protein]]
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[[Category: Fritzsch G]]
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[[Category: Fritzsch, G.]]
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[[Category: Koepke J]]
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[[Category: Koepke, J.]]
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[[Category: Luecke C]]
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[[Category: Luecke, C.]]
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[[Category: Rueterjans H]]
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[[Category: Rueterjans, H.]]
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[[Category: Scharff EI]]
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[[Category: Scharff, E I.]]
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[[Category: Beta-propeller]]
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[[Category: Calcium-binding site]]
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[[Category: Selenometionine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:32:06 2008''
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Crystal structure of DFPase from Loligo vulgaris

PDB ID 1e1a

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