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| | ==The crystal structure of D-mandelate dehydrogenase== | | ==The crystal structure of D-mandelate dehydrogenase== |
| - | <StructureSection load='3wfi' size='340' side='right' caption='[[3wfi]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3wfi' size='340' side='right'caption='[[3wfi]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wfi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19434 Atcc 19434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WFI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wfi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wfj|3wfj]]</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]] 1.997Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pLG1-0150 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 ATCC 19434])</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=3wfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfi OCA], [https://pdbe.org/3wfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfi RCSB], [https://www.ebi.ac.uk/pdbsum/3wfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfi 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/2-dehydropantoate_2-reductase 2-dehydropantoate 2-reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.169 1.1.1.169] </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=3wfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfi OCA], [http://pdbe.org/3wfi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wfi RCSB], [http://www.ebi.ac.uk/pdbsum/3wfi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/E3USM3_ENTFC E3USM3_ENTFC]] Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid (By similarity).[RuleBase:RU003776] | + | [https://www.uniprot.org/uniprot/E3USM3_ENTFC E3USM3_ENTFC] Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid (By similarity).[RuleBase:RU003776] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3wfi" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3wfi" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Mandelate dehydrogenase|Mandelate dehydrogenase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2-dehydropantoate 2-reductase]] | + | [[Category: Enterococcus faecium]] |
| - | [[Category: Atcc 19434]] | + | [[Category: Large Structures]] |
| - | [[Category: Arai, K]] | + | [[Category: Arai K]] |
| - | [[Category: Fujisawa, S]] | + | [[Category: Fujisawa S]] |
| - | [[Category: Furukawa, N]] | + | [[Category: Furukawa N]] |
| - | [[Category: Miyanaga, A]] | + | [[Category: Miyanaga A]] |
| - | [[Category: Nakajima, M]] | + | [[Category: Nakajima M]] |
| - | [[Category: Taguchi, H]] | + | [[Category: Taguchi H]] |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Nadh binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rosmann fold]]
| + | |
| Structural highlights
Function
E3USM3_ENTFC Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid (By similarity).[RuleBase:RU003776]
Publication Abstract from PubMed
D-Mandelate dehydrogenases (D-ManDHs), belonging to a new d-2-hydroxyacid dehydrogenase family, catalyze the conversion between benzoylformate and d-mandelate using NAD as a coenzyme. We determined the first D-ManDH structure, that of ManDH2 from Enterococcus faecalis IAM10071. The overall structure showed ManDH2 has a similar fold to 2-ketopantoate reductase (KPR), which catalyzes the conversion of 2-ketopantoate to d-pantoate using NADP as a coenzyme. They share conserved catalytic residues, indicating ManDH2 has the same reaction mechanism as KPR. However, ManDH2 exhibits significant structural variations in the coenzyme and substrate binding sites compared to KPR. These structural observations could explain their different coenzyme and substrate specificities.
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.,Miyanaga A, Fujisawa S, Furukawa N, Arai K, Nakajima M, Taguchi H Biochem Biophys Res Commun. 2013 Sep 13;439(1):109-14. doi:, 10.1016/j.bbrc.2013.08.019. Epub 2013 Aug 13. PMID:23954635[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miyanaga A, Fujisawa S, Furukawa N, Arai K, Nakajima M, Taguchi H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem Biophys Res Commun. 2013 Sep 13;439(1):109-14. doi:, 10.1016/j.bbrc.2013.08.019. Epub 2013 Aug 13. PMID:23954635 doi:http://dx.doi.org/10.1016/j.bbrc.2013.08.019
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