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| | <StructureSection load='1gu0' size='340' side='right'caption='[[1gu0]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1gu0' size='340' side='right'caption='[[1gu0]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gu0]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GU0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gu0]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GU0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d0i|1d0i]], [[1gqn|1gqn]], [[1gqo|1gqo]], [[1gtz|1gtz]], [[1gu1|1gu1]], [[2dhq|2dhq]], [[1qfe|1qfe]], [[1guy|1guy]], [[1gvz|1gvz]], [[1gv1|1gv1]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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_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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu0 OCA], [https://pdbe.org/1gu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu0 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=1gu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu0 OCA], [http://pdbe.org/1gu0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gu0 RCSB], [http://www.ebi.ac.uk/pdbsum/1gu0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AROQ_STRCO AROQ_STRCO]] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169] | + | [https://www.uniprot.org/uniprot/AROQ_STRCO AROQ_STRCO] 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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coggins, J R]] | + | [[Category: Streptomyces coelicolor]] |
| - | [[Category: Hunter, I S]] | + | [[Category: Coggins JR]] |
| - | [[Category: Krell, T]] | + | [[Category: Hunter IS]] |
| - | [[Category: Lapthorn, A J]] | + | [[Category: Krell T]] |
| - | [[Category: Robinson, D]] | + | [[Category: Lapthorn AJ]] |
| - | [[Category: Roszak, A W]] | + | [[Category: Robinson D]] |
| - | [[Category: Dodecameric quaternary structure]]
| + | [[Category: Roszak AW]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| - | [[Category: Tetrahedral symmetry]]
| + | |
| - | [[Category: Type ii dehydroquinase]]
| + | |
| Structural highlights
Function
AROQ_STRCO 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 DHQase from Streptomyces coelicolor has been solved and refined to high resolution in complexes with a number of ligands, including dehydroshikimate and a rationally designed transition state analogue, 2,3-anhydro-quinic acid. These structures define the active site of the enzyme and the role of key amino acid residues and provide snap shots of the catalytic cycle. The resolution of the flexible lid domain (residues 21-31) shows that the invariant residues Arg23 and Tyr28 close over the active site cleft. The tyrosine acts as the base in the initial proton abstraction, and evidence is provided that the reaction proceeds via an enol intermediate. The active site of the structure of DHQase in complex with the transition state analog also includes molecules of tartrate and glycerol, which provide a basis for further inhibitor design.
The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor.,Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ Structure. 2002 Apr;10(4):493-503. PMID:11937054[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ. The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor. Structure. 2002 Apr;10(4):493-503. PMID:11937054
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