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| | <StructureSection load='1uqr' size='340' side='right'caption='[[1uqr]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1uqr' size='340' side='right'caption='[[1uqr]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uqr]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Actpl Actpl]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UQR FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] </span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqr OCA], [http://pdbe.org/1uqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uqr RCSB], [http://www.ebi.ac.uk/pdbsum/1uqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqr ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AROQ_ACTPL AROQ_ACTPL]] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169] | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-dehydroquinate dehydratase]] | + | [[Category: Actinobacillus pleuropneumoniae]] |
| - | [[Category: Actpl]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Afonina, E]] | + | [[Category: Afonina E]] |
| - | [[Category: Bondt, H De]] | + | [[Category: De Bondt H]] |
| - | [[Category: Garcia-Ruiz, J M]] | + | [[Category: Garcia-Ruiz JM]] |
| - | [[Category: Gonzalez-Ramirez, L A]] | + | [[Category: Gonzalez-Ramirez LA]] |
| - | [[Category: Gulnik, S]] | + | [[Category: Gulnik S]] |
| - | [[Category: Lopez-Jaramillo, J]] | + | [[Category: Lopez-Jaramillo J]] |
| - | [[Category: Maes, D]] | + | [[Category: Maes D]] |
| - | [[Category: Yu, B]] | + | [[Category: Yu B]] |
| - | [[Category: Zegers, I]] | + | [[Category: Zegers I]] |
| - | [[Category: Aromatic amino acid biosynthesis]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| Structural highlights
Function
AROQ_ACTPL Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maes D, Gonzalez-Ramirez LA, Lopez-Jaramillo J, Yu B, De Bondt H, Zegers I, Afonina E, Garcia-Ruiz JM, Gulnik S. Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):463-71. Epub 2004, Feb 25. PMID:14993670 doi:10.1107/S090744490302969X
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