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| | ==Crystal structure of 3-dehydroquinate synthase (DHQS)from Helicobacter pylori== | | ==Crystal structure of 3-dehydroquinate synthase (DHQS)from Helicobacter pylori== |
| - | <StructureSection load='3clh' size='340' side='right' caption='[[3clh]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='3clh' size='340' side='right'caption='[[3clh]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3clh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CLH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3clh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CLH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aroB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr> | + | <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=ZN:ZINC+ION'>ZN</scene></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_synthase 3-dehydroquinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.4 4.2.3.4] </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=3clh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3clh OCA], [https://pdbe.org/3clh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3clh RCSB], [https://www.ebi.ac.uk/pdbsum/3clh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3clh ProSAT]</span></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=3clh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3clh OCA], [http://pdbe.org/3clh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3clh RCSB], [http://www.ebi.ac.uk/pdbsum/3clh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3clh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AROB_HELPY AROB_HELPY] |
| | == 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 synthase]] | + | [[Category: Helicobacter pylori]] |
| - | [[Category: Atcc 43504]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, Y C]] | + | [[Category: Chen YC]] |
| - | [[Category: Cheng, W C]] | + | [[Category: Cheng WC]] |
| - | [[Category: Liu, J S]] | + | [[Category: Liu JS]] |
| - | [[Category: Wang, H J]] | + | [[Category: Wang HJ]] |
| - | [[Category: Wang, W C]] | + | [[Category: Wang WC]] |
| - | [[Category: Amino-acid biosynthesis]]
| + | |
| - | [[Category: Aromatic amino acid biosynthesis]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Dhq]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| Structural highlights
Function
AROB_HELPY
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
Dehydroquinate synthase (DHQS) is a nicotinamide adenine dinucleotide (NAD)-dependent enzyme that converts 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) into 3-dehydroquinate (DHQ). Since it catalyzes the second key step in the shikimate pathway, which is crucial for the aromatic amino acid metabolism in bacteria, fungi, and plants, but not in mammals, DHQS is a potential target for new antimicrobial agents, anti-parasitic agents and herbicides. The crystal structure of Helicobacter pylori DHQS (HpDHQS) complexed with NAD has been determined at 2.4-A resolution and was found to possess an N-terminal Rossmann-fold domain and a C-terminal alpha-helical domain. Structural comparison reveals that the binary complex adopts an open-state conformation and shares conserved residues in the binding pocket. Virtual docking of compounds into the active site of the HpDHQS structure using the GOLD docking program led to the identification of several inhibitors. The most active compound had an IC(50) value of 61 microM, which may serve as a lead for potent inhibitors.
Structure-based inhibitor discovery of Helicobacter pylori dehydroquinate synthase.,Liu JS, Cheng WC, Wang HJ, Chen YC, Wang WC Biochem Biophys Res Commun. 2008 Aug 15;373(1):1-7. Epub 2008 May 27. PMID:18503755[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu JS, Cheng WC, Wang HJ, Chen YC, Wang WC. Structure-based inhibitor discovery of Helicobacter pylori dehydroquinate synthase. Biochem Biophys Res Commun. 2008 Aug 15;373(1):1-7. Epub 2008 May 27. PMID:18503755 doi:10.1016/j.bbrc.2008.05.070
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