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| | <StructureSection load='4a7z' size='340' side='right'caption='[[4a7z]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='4a7z' size='340' side='right'caption='[[4a7z]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a7z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysosporium_pruinosum_(gilman_&_abbott)_carmich. Chrysosporium pruinosum (gilman & abbott) carmich.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A7Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A7Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a7z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A7Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AY9:ASCOPYRONE+M'>AY9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a7k|4a7k]], [[4a7y|4a7y]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AY9:ASCOPYRONE+M'>AY9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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/Aldos-2-ulose_dehydratase Aldos-2-ulose dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.110 4.2.1.110] </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=4a7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a7z OCA], [https://pdbe.org/4a7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a7z RCSB], [https://www.ebi.ac.uk/pdbsum/4a7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a7z 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=4a7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a7z OCA], [http://pdbe.org/4a7z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a7z RCSB], [http://www.ebi.ac.uk/pdbsum/4a7z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a7z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AUD_PHACH AUD_PHACH]] A bifunctional enzyme which catalyzes the dehydration of anhydrofructose into ascopyrone M, and the isomerization of ascopyrone M into microthecin. The dehydration of anhydrofructose is the primary function.<ref>PMID:15716041</ref> | + | [https://www.uniprot.org/uniprot/AUD_PHACH AUD_PHACH] A bifunctional enzyme which catalyzes the dehydration of anhydrofructose into ascopyrone M, and the isomerization of ascopyrone M into microthecin. The dehydration of anhydrofructose is the primary function.<ref>PMID:15716041</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aldos-2-ulose dehydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Claesson, M]] | + | [[Category: Phanerodontia chrysosporium]] |
| - | [[Category: Fiskesund, R]] | + | [[Category: Claesson M]] |
| - | [[Category: Lindqvist, Y]] | + | [[Category: Fiskesund R]] |
| - | [[Category: Madrid, S]] | + | [[Category: Lindqvist Y]] |
| - | [[Category: Sandalova, T]] | + | [[Category: Madrid S]] |
| - | [[Category: Schneider, G]] | + | [[Category: Sandalova T]] |
| - | [[Category: Yu, S]] | + | [[Category: Schneider G]] |
| - | [[Category: Cortalcerone/microthecin forming]]
| + | [[Category: Yu S]] |
| - | [[Category: Dehydratase/isomerase]]
| + | |
| - | [[Category: Lignin degradation]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Metalloenzyme]]
| + | |
| Structural highlights
Function
AUD_PHACH A bifunctional enzyme which catalyzes the dehydration of anhydrofructose into ascopyrone M, and the isomerization of ascopyrone M into microthecin. The dehydration of anhydrofructose is the primary function.[1]
Publication Abstract from PubMed
The enzyme aldos-2-ulose dehydratase/isomerase (AUDH) participates in carbohydrate secondary metabolism, catalyzing the conversion of glucosone and 1,5-d-anhydrofructose to the secondary metabolites cortalcerone and microthecin, respectively. AUDH is a homo-dimeric enzyme with subunits of 900 amino acids. The subunit consists of a seven-bladed beta-propeller domain, two cupin folds and a C-terminal lectin domain. AUDH contains a structural Zn(2+) and Mg(2+) located in loop regions and two zinc ions at the bottom of two putative active-site clefts in the propeller and the cupin domain, respectively. Catalysis is dependent on these two zinc ions, as their specific removal led to loss of enzymatic activity. The structure of the Zn(2)(+)-depleted enzyme is very similar to that of native AUDH, and structural changes upon metal removal as the cause for the catalytic deficiencies can be excluded. The complex with the reaction intermediate ascopyrone M shows binding of this compound at two different sites, with direct coordination to Zn(2+) in the propeller domain and as second sphere ligand of the metal ion in the cupin domain. These observations suggest that the two reactions of AUDH might be catalyzed in two different active sites, about 60 A apart. The dehydration reaction most likely follows an elimination mechanism, where Zn(2+) acts as a Lewis acid polarizing the C2 keto group of 1,5-d-anhydrofructose. Abstraction of the proton at the C3 carbon atom and protonation of the leaving group, the C4 hydroxyl moiety, could potentially be catalyzed by the side chain of the suitably positioned residue His155.
Crystal Structure of Bifunctional Aldos-2-Ulose Dehydratase/Isomerase from Phanerochaete chrysosporium with the Reaction Intermediate Ascopyrone M.,Claesson M, Lindqvist Y, Madrid S, Sandalova T, Fiskesund R, Yu S, Schneider G J Mol Biol. 2012 Apr 6;417(4):279-93. Epub 2012 Feb 8. PMID:22330145[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yu S. Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate. Biochim Biophys Acta. 2005 May 25;1723(1-3):63-73. Epub 2005 Jan 25. PMID:15716041 doi:http://dx.doi.org/10.1016/j.bbagen.2005.01.004
- ↑ Claesson M, Lindqvist Y, Madrid S, Sandalova T, Fiskesund R, Yu S, Schneider G. Crystal Structure of Bifunctional Aldos-2-Ulose Dehydratase/Isomerase from Phanerochaete chrysosporium with the Reaction Intermediate Ascopyrone M. J Mol Biol. 2012 Apr 6;417(4):279-93. Epub 2012 Feb 8. PMID:22330145 doi:10.1016/j.jmb.2012.02.001
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