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| | <StructureSection load='4ynu' size='340' side='right'caption='[[4ynu]], [[Resolution|resolution]] 1.57Å' scene=''> | | <StructureSection load='4ynu' size='340' side='right'caption='[[4ynu]], [[Resolution|resolution]] 1.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ynu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfn Aspfn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YNU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ynu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus_NRRL3357 Aspergillus flavus NRRL3357]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YNU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=LGC:(3S,4R,5R,6S)-3,4,5-TRIHYDROXY-6-(HYDROXYMETHYL)TETRAHYDRO-2H-PYRAN-2-ONE'>LGC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=LGC:(3S,4R,5R,6S)-3,4,5-TRIHYDROXY-6-(HYDROXYMETHYL)TETRAHYDRO-2H-PYRAN-2-ONE'>LGC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ynt|4ynt]]</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=4ynu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ynu OCA], [https://pdbe.org/4ynu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ynu RCSB], [https://www.ebi.ac.uk/pdbsum/4ynu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ynu ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFLA_076820 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=332952 ASPFN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose_1-dehydrogenase_(FAD,_quinone) Glucose 1-dehydrogenase (FAD, quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.5.9 1.1.5.9] </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=4ynu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ynu OCA], [http://pdbe.org/4ynu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ynu RCSB], [http://www.ebi.ac.uk/pdbsum/4ynu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ynu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B8MX95_ASPFN B8MX95_ASPFN] |
| | <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: Aspfn]] | + | [[Category: Aspergillus flavus NRRL3357]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kamitori, S]] | + | [[Category: Kamitori S]] |
| - | [[Category: Kojima, K]] | + | [[Category: Kojima K]] |
| - | [[Category: Sakai, G]] | + | [[Category: Sakai G]] |
| - | [[Category: Sode, K]] | + | [[Category: Sode K]] |
| - | [[Category: Yoshida, H]] | + | [[Category: Yoshida H]] |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Glucose dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
B8MX95_ASPFN
Publication Abstract from PubMed
We report the first three-dimensional structure of fungus-derived glucose dehydrogenase using flavin adenine dinucleotide (FAD) as the cofactor. This is currently the most advanced and popular enzyme used in glucose sensor strips manufactured for glycemic control by diabetic patients. We prepared recombinant nonglycosylated FAD-dependent glucose dehydrogenase (FADGDH) derived from Aspergillus flavus (AfGDH) and obtained the X-ray structures of the binary complex of enzyme and reduced FAD at a resolution of 1.78 A and the ternary complex with reduced FAD and D-glucono-1,5-lactone (LGC) at a resolution of 1.57 A. The overall structure is similar to that of fungal glucose oxidases (GOxs) reported till date. The ternary complex with reduced FAD and LGC revealed the residues recognizing the substrate. His505 and His548 were subjected for site-directed mutagenesis studies, and these two residues were revealed to form the catalytic pair, as those conserved in GOxs. The absence of residues that recognize the sixth hydroxyl group of the glucose of AfGDH, and the presence of significant cavity around the active site may account for this enzyme activity toward xylose. The structural information will contribute to the further engineering of FADGDH for use in more reliable and economical biosensing technology for diabetes management.
Structural analysis of fungus-derived FAD glucose dehydrogenase.,Yoshida H, Sakai G, Mori K, Kojima K, Kamitori S, Sode K Sci Rep. 2015 Aug 27;5:13498. doi: 10.1038/srep13498. PMID:26311535[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yoshida H, Sakai G, Mori K, Kojima K, Kamitori S, Sode K. Structural analysis of fungus-derived FAD glucose dehydrogenase. Sci Rep. 2015 Aug 27;5:13498. doi: 10.1038/srep13498. PMID:26311535 doi:http://dx.doi.org/10.1038/srep13498
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