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| ==Crystal structure of an Ael1 enzyme from Pseudomonas putida== | | ==Crystal structure of an Ael1 enzyme from Pseudomonas putida== |
| <StructureSection load='3pwz' size='340' side='right' caption='[[3pwz]], [[Resolution|resolution]] 1.71Å' scene=''> | | <StructureSection load='3pwz' size='340' side='right'caption='[[3pwz]], [[Resolution|resolution]] 1.71Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3pwz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PWZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PWZ FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3pwz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PWZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PWZ FirstGlance]. <br> |
| </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ael1, aroE-2, aroE3, PP3002, PP_3002 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida])</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]] 1.705Å</td></tr> |
| <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] </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=3pwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pwz OCA], [https://pdbe.org/3pwz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pwz RCSB], [https://www.ebi.ac.uk/pdbsum/3pwz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pwz ProSAT]</span></td></tr> |
| <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pwz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pwz RCSB], [http://www.ebi.ac.uk/pdbsum/3pwz PDBsum]</span></td></tr>
| | </table> |
| <table> | | == Function == |
| <div style="background-color:#fffaf0;">
| | [https://www.uniprot.org/uniprot/Q88IJ7_PSEPK Q88IJ7_PSEPK] |
| == Publication Abstract from PubMed == | |
| Shikimate dehydrogenase (SDH) catalyzes the reversible NADPH-dependent reduction of 3-dehydroshikimate to shikimate. This reaction represents the fourth step of the shikimate pathway, the essential route for the biosynthesis of the aromatic amino acids in plants, fungi, bacteria, and apicomplexan parasites. The absence of this pathway in animals makes it an attractive target for herbicides and antimicrobials. At least four functionally distinct enzyme classes, AroE, YdiB, SDH-like (SdhL), and AroE-like1 (Ael1), utilize shikimate as a substrate in vitro and form the SDH family. Crystal structures have been determined for AroE, YdiB, and SdhL. In this study, we have determined the first representative crystal structure of an Ael1 enzyme. We demonstrate that Ael1 shares a similar overall structure with the other members of the SDH family. This high level of structural conservation extends to the active sites of the enzymes. In particular, an ionizable active site lysine and aspartate are present in all SDH homologues. Two distinct biochemical roles have been reported for this Lys-Asp pair: as binding residues in YdiB and as a catalytic dyad in AroE and SdhL. Here, we establish that the residues function as a catalytic dyad in Ael1 and, interestingly, in at least one YdiB homologue. The conservation of three-dimensional fold, active site architecture, and catalytic mechanism among members of the SDH family will facilitate the design of drugs targeting the shikimate pathway.
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| Structural and Mechanistic Analysis of a Novel Class of Shikimate Dehydrogenases: Evidence for a Conserved Catalytic Mechanism in the Shikimate Dehydrogenase Family.,Peek J, Lee J, Hu S, Senisterra G, Christendat D Biochemistry. 2011 Sep 15. PMID:21846128<ref>PMID:21846128</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Shikimate dehydrogenase|Shikimate dehydrogenase]] | | *[[Shikimate dehydrogenase 3D structures|Shikimate dehydrogenase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Pseudomonas putida]] | | [[Category: Pseudomonas putida]] |
| [[Category: Shikimate dehydrogenase]]
| | [[Category: Christendat D]] |
| [[Category: Christendat, D.]] | | [[Category: Peek J]] |
| [[Category: Peek, J.]] | |
| [[Category: Alpha-beta]]
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| [[Category: Enzyme]]
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| [[Category: Oxidoreductase]]
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| [[Category: Shikimate dehydrogenase]]
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