3hlh

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{{Seed}}
 
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[[Image:3hlh.png|left|200px]]
 
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==Diisopropyl fluorophosphatase (DFPase), active site mutants==
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The line below this paragraph, containing "STRUCTURE_3hlh", creates the "Structure Box" on the page.
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<StructureSection load='3hlh' size='340' side='right'caption='[[3hlh]], [[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'>[[3hlh]] is a 4 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=3HLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HLH FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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_3hlh| PDB=3hlh | 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=3hlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hlh OCA], [https://pdbe.org/3hlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hlh RCSB], [https://www.ebi.ac.uk/pdbsum/3hlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hlh 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/hl/3hlh_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=3hlh 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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Diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is an efficient and robust biocatalyst for the hydrolysis of a range of highly toxic organophosphorus compounds including the nerve agents sarin, soman, and cyclosarin. In contrast to the substrate diisopropyl fluorophosphate (DFP) the nerve agents possess an asymmetric phosphorus atom, which leads to pairs of enantiomers that display markedly different toxicities. Wild-type DFPase prefers the less toxic stereoisomers of the substrates which leads to slower detoxification despite rapid hydrolysis. Enzyme engineering efforts based on rational design yielded two quadruple enzyme mutants with reversed enantioselectivity and overall enhanced activity against tested nerve agents. The reversed stereochemical preference is explained through modeling studies and the crystal structures of the two mutants. Using the engineered mutants in combination with wild-type DFPase leads to significantly enhanced activity and detoxification, which is especially important for personal decontamination. Our findings may also be of relevance for the structurally related enzyme human paraoxonase (PON), which is of considerable interest as a potential catalytic in vivo scavenger in case of organophosphorus poisoning.
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===Diisopropyl fluorophosphatase (DFPase), active site mutants===
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Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design.,Melzer M, Chen JC, Heidenreich A, Gab J, Koller M, Kehe K, Blum MM J Am Chem Soc. 2009 Dec 2;131(47):17226-32. PMID:19894712<ref>PMID:19894712</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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The line below this paragraph, {{ABSTRACT_PUBMED_19894712}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3hlh" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19894712 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19894712}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3HLH is a 4 chains structure of sequences 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=3HLH OCA].
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==Reference==
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<ref group="xtra">PMID:19894712</ref><references group="xtra"/>
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[[Category: Diisopropyl-fluorophosphatase]]
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[[Category: Loligo vulgaris]]
[[Category: Loligo vulgaris]]
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[[Category: Blum, M M.]]
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[[Category: Blum M-M]]
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[[Category: Chen, J C.H.]]
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[[Category: Chen JC-H]]
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[[Category: Beta propeller]]
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[[Category: Calcium]]
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[[Category: Calcium binding]]
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[[Category: Hydrolase]]
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[[Category: Metal-binding]]
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[[Category: Phosphotriesterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 9 14:21:06 2009''
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Current revision

Diisopropyl fluorophosphatase (DFPase), active site mutants

PDB ID 3hlh

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