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| | <StructureSection load='4l8l' size='340' side='right'caption='[[4l8l]], [[Resolution|resolution]] 1.74Å' scene=''> | | <StructureSection load='4l8l' size='340' side='right'caption='[[4l8l]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4l8l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L8L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L8L FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aroQ, aroQ1, PA4846 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr> | + | </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=4l8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l8l OCA], [https://pdbe.org/4l8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l8l RCSB], [https://www.ebi.ac.uk/pdbsum/4l8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l8l ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l8l OCA], [http://pdbe.org/4l8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l8l RCSB], [http://www.ebi.ac.uk/pdbsum/4l8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l8l ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AROQ1_PSEAE AROQ1_PSEAE]] Catalyzes a trans-dehydration via an enolate intermediate (By similarity). | + | [https://www.uniprot.org/uniprot/AROQ1_PSEAE AROQ1_PSEAE] Catalyzes a trans-dehydration via an enolate intermediate (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Dehydroquinase|Dehydroquinase]] | + | *[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-dehydroquinate dehydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Asojo, O A]] | + | [[Category: Asojo OA]] |
| - | [[Category: Reiling, S A]] | + | [[Category: Reiling SA]] |
| - | [[Category: Alpha helix]]
| + | |
| - | [[Category: Beta sheet]]
| + | |
| - | [[Category: Dehydratase]]
| + | |
| - | [[Category: Dehydroquinic acid]]
| + | |
| - | [[Category: Flavodoxin-like fold]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
AROQ1_PSEAE Catalyzes a trans-dehydration via an enolate intermediate (By similarity).
Publication Abstract from PubMed
Pseudomonas aeruginosa causes opportunistic infections and is resistant to most antibiotics. Ongoing efforts to generate much-needed new antibiotics include targeting enzymes that are vital for P. aeruginosa but are absent in mammals. One such enzyme, type II dehydroquinase (DHQase), catalyzes the interconversion of 3-dehydroquinate and 3-dehydroshikimate, a necessary step in the shikimate pathway. This step is vital for the proper synthesis of phenylalanine, tryptophan, tyrosine and other aromatic metabolites. The recombinant expression, purification and crystal structure of catalytically active DHQase from P. aeruginosa (PaDHQase) are presented. Cubic crystals belonging to space group F23, with unit-cell parameters a = b = c = 125.39 A, were obtained by vapor diffusion in sitting drops and the structure was refined to an R factor of 16% at 1.74 A resolution. PaDHQase is a prototypical type II DHQase with the classical flavodoxin-like alpha/beta topology.
Structure of type II dehydroquinase from Pseudomonas aeruginosa.,Reiling S, Kelleher A, Matsumoto MM, Robinson G, Asojo OA Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1485-91. doi:, 10.1107/S2053230X14020214. Epub 2014 Oct 25. PMID:25372814[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reiling S, Kelleher A, Matsumoto MM, Robinson G, Asojo OA. Structure of type II dehydroquinase from Pseudomonas aeruginosa. Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1485-91. doi:, 10.1107/S2053230X14020214. Epub 2014 Oct 25. PMID:25372814 doi:http://dx.doi.org/10.1107/S2053230X14020214
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