2o2s

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[[Image:2o2s.jpg|left|200px]]
 
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==The structure of T. gondii enoyl acyl carrier protein reductase in complex with NAD and triclosan==
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The line below this paragraph, containing "STRUCTURE_2o2s", creates the "Structure Box" on the page.
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<StructureSection load='2o2s' size='340' side='right'caption='[[2o2s]], [[Resolution|resolution]] 2.60&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'>[[2o2s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii_RH Toxoplasma gondii RH]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O2S 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]] 2.6&#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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr>
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{{STRUCTURE_2o2s| PDB=2o2s | 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=2o2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o2s OCA], [https://pdbe.org/2o2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o2s RCSB], [https://www.ebi.ac.uk/pdbsum/2o2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o2s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q6UCJ9_TOXGO Q6UCJ9_TOXGO]
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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/o2/2o2s_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=2o2s 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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Recent studies have demonstrated that submicromolar concentrations of the biocide triclosan arrest the growth of the apicomplexan parasites Plasmodium falciparum and Toxoplasma gondii and inhibit the activity of the apicomplexan enoyl acyl carrier protein reductase (ENR). The crystal structures of T. gondii and P. falciparum ENR in complex with NAD(+) and triclosan and of T. gondii ENR in an apo form have been solved to 2.6, 2.2 and 2.8 A, respectively. The structures of T. gondii ENR have revealed that, as in its bacterial and plant homologues, a loop region which flanks the active site becomes ordered upon inhibitor binding, resulting in the slow tight binding of triclosan. In addition, the T. gondii ENR-triclosan complex reveals the folding of a hydrophilic insert common to the apicomplexan family that flanks the substrate-binding domain and is disordered in all other reported apicomplexan ENR structures. Structural comparison of the apicomplexan ENR structures with their bacterial and plant counterparts has revealed that although the active sites of the parasite enzymes are broadly similar to those of their bacterial counterparts, there are a number of important differences within the drug-binding pocket that reduce the packing interactions formed with several inhibitors in the apicomplexan ENR enzymes. Together with other significant structural differences, this provides a possible explanation of the lower affinity of the parasite ENR enzyme family for aminopyridine-based inhibitors, suggesting that an effective antiparasitic agent may well be distinct from equivalent antimicrobials.
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'''The structure of T. gondii enoyl acyl carrier protein reductase in complex with NAD and triclosan'''
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Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents.,Muench SP, Prigge ST, McLeod R, Rafferty JB, Kirisits MJ, Roberts CW, Mui EJ, Rice DW Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):328-38. Epub 2007, Feb 21. PMID:17327670<ref>PMID:17327670</ref>
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==Overview==
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Recent studies have demonstrated that submicromolar concentrations of the biocide triclosan arrest the growth of the apicomplexan parasites Plasmodium falciparum and Toxoplasma gondii and inhibit the activity of the apicomplexan enoyl acyl carrier protein reductase (ENR). The crystal structures of T. gondii and P. falciparum ENR in complex with NAD(+) and triclosan and of T. gondii ENR in an apo form have been solved to 2.6, 2.2 and 2.8 A, respectively. The structures of T. gondii ENR have revealed that, as in its bacterial and plant homologues, a loop region which flanks the active site becomes ordered upon inhibitor binding, resulting in the slow tight binding of triclosan. In addition, the T. gondii ENR-triclosan complex reveals the folding of a hydrophilic insert common to the apicomplexan family that flanks the substrate-binding domain and is disordered in all other reported apicomplexan ENR structures. Structural comparison of the apicomplexan ENR structures with their bacterial and plant counterparts has revealed that although the active sites of the parasite enzymes are broadly similar to those of their bacterial counterparts, there are a number of important differences within the drug-binding pocket that reduce the packing interactions formed with several inhibitors in the apicomplexan ENR enzymes. Together with other significant structural differences, this provides a possible explanation of the lower affinity of the parasite ENR enzyme family for aminopyridine-based inhibitors, suggesting that an effective antiparasitic agent may well be distinct from equivalent antimicrobials.
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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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2O2S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O2S OCA].
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</div>
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<div class="pdbe-citations 2o2s" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents., Muench SP, Prigge ST, McLeod R, Rafferty JB, Kirisits MJ, Roberts CW, Mui EJ, Rice DW, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):328-38. Epub 2007, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17327670 17327670]
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*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
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[[Category: Single protein]]
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== References ==
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[[Category: Toxoplasma gondii]]
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<references/>
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[[Category: Kirisits, M J.]]
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__TOC__
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[[Category: McLeod, R.]]
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</StructureSection>
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[[Category: Muench, S P.]]
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[[Category: Large Structures]]
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[[Category: Mui, E J.]]
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[[Category: Toxoplasma gondii RH]]
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[[Category: Prigge, S T.]]
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[[Category: Kirisits MJ]]
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[[Category: Rafferty, J B.]]
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[[Category: McLeod R]]
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[[Category: Rice, D W.]]
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[[Category: Muench SP]]
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[[Category: Roberts, C W.]]
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[[Category: Mui EJ]]
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[[Category: Enoyl reductase]]
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[[Category: Prigge ST]]
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[[Category: Rossmann fold]]
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[[Category: Rafferty JB]]
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[[Category: Triclosan]]
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[[Category: Rice DW]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:15:05 2008''
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[[Category: Roberts CW]]

Current revision

The structure of T. gondii enoyl acyl carrier protein reductase in complex with NAD and triclosan

PDB ID 2o2s

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