1uqr
From Proteopedia
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| - | [[Image:1uqr.gif|left|200px]]<br /><applet load="1uqr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1uqr, resolution 1.7Å" /> | ||
| - | '''TYPE II 3-DEHYDROQUINATE DEHYDRATASE (DHQASE) FROM ACTINOBACILLUS PLEUROPNEUMONIAE'''<br /> | ||
| - | == | + | ==Type II 3-dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae== |
| + | <StructureSection load='1uqr' size='340' side='right'caption='[[1uqr]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1uqr]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinobacillus_pleuropneumoniae Actinobacillus pleuropneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UQR FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqr OCA], [https://pdbe.org/1uqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uqr RCSB], [https://www.ebi.ac.uk/pdbsum/1uqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AROQ_ACTPL AROQ_ACTPL] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uq/1uqr_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1uqr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The structure of the type II dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae, the third enzyme of the shikimate pathway, has been determined. Crystals diffracting to 1.7 A were obtained in space and on earth using the counter-diffusion technique. The structure was solved using molecular replacement and refined to high resolution. The overall structure of the dodecameric enzyme is described and compared with structures of DHQases from other bacteria. DHQases contain a flexible loop that presumably closes over the active site upon substrate binding. The enzyme can exist in an open or closed conformation. The present structure displays the open conformation, with a sulfate anion bound in the active site. The availability of this structure opens a route to structure-based antibiotics targetting this pathogenic bacterium. | The structure of the type II dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae, the third enzyme of the shikimate pathway, has been determined. Crystals diffracting to 1.7 A were obtained in space and on earth using the counter-diffusion technique. The structure was solved using molecular replacement and refined to high resolution. The overall structure of the dodecameric enzyme is described and compared with structures of DHQases from other bacteria. DHQases contain a flexible loop that presumably closes over the active site upon substrate binding. The enzyme can exist in an open or closed conformation. The present structure displays the open conformation, with a sulfate anion bound in the active site. The availability of this structure opens a route to structure-based antibiotics targetting this pathogenic bacterium. | ||
| - | + | Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae.,Maes D, Gonzalez-Ramirez LA, Lopez-Jaramillo J, Yu B, De Bondt H, Zegers I, Afonina E, Garcia-Ruiz JM, Gulnik S Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):463-71. Epub 2004, Feb 25. PMID:14993670<ref>PMID:14993670</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1uqr" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Actinobacillus pleuropneumoniae]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Afonina E]] | ||
| + | [[Category: De Bondt H]] | ||
| + | [[Category: Garcia-Ruiz JM]] | ||
| + | [[Category: Gonzalez-Ramirez LA]] | ||
| + | [[Category: Gulnik S]] | ||
| + | [[Category: Lopez-Jaramillo J]] | ||
| + | [[Category: Maes D]] | ||
| + | [[Category: Yu B]] | ||
| + | [[Category: Zegers I]] | ||
Current revision
Type II 3-dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae
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