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| | <StructureSection load='2vfu' size='340' side='right'caption='[[2vfu]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2vfu' size='340' side='right'caption='[[2vfu]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vfu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VFU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VFU FirstGlance]. <br> |
| - | </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=MTL:D-MANNITOL'>MTL</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vfr|2vfr]], [[2vfs|2vfs]], [[2vft|2vft]], [[2vfv|2vfv]]</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=MTL:D-MANNITOL'>MTL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alditol_oxidase Alditol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.41 1.1.3.41] </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=2vfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfu OCA], [https://pdbe.org/2vfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vfu RCSB], [https://www.ebi.ac.uk/pdbsum/2vfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfu OCA], [http://pdbe.org/2vfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vfu RCSB], [http://www.ebi.ac.uk/pdbsum/2vfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYOA_STRCO XYOA_STRCO] Oxidase that performs selective oxidation of the terminal primary hydroxyl group of several alditols, with a reduction of O2 to H2O2. Shows highest activity on xylitol and D-sorbitol, and a poor efficiency with D-mannitol and L-threitol.<ref>PMID:17517896</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alditol oxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strco]]
| + | [[Category: Forneris F]] |
| - | [[Category: Forneris, F]] | + | [[Category: Mattevi A]] |
| - | [[Category: Mattevi, A]] | + | |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Flavin]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Polyol]]
| + | |
| - | [[Category: Sugar]]
| + | |
| Structural highlights
Function
XYOA_STRCO Oxidase that performs selective oxidation of the terminal primary hydroxyl group of several alditols, with a reduction of O2 to H2O2. Shows highest activity on xylitol and D-sorbitol, and a poor efficiency with D-mannitol and L-threitol.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Alditol oxidase (AldO) from Streptomyces coelicolor A3(2) is a soluble monomeric flavin-dependent oxidase that performs selective oxidation of the terminal primary hydroxyl group of several alditols. Here, we report the crystal structure of the recombinant enzyme in its native state and in complex with both six-carbon (mannitol and sorbitol) and five-carbon substrates (xylitol). AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes and exhibits a covalently linked FAD which is located at the bottom of a funnel-shaped pocket that forms the active site. The high resolution of the three-dimensional structures highlights a well-defined hydrogen-bonding network that tightly constrains the substrate in the productive conformation for catalysis. Substrate binding occurs through a lock-and-key mechanism and does not induce conformational changes with respect to the ligand-free protein. A network of charged residues is proposed to favor catalysis through stabilization of the deprotonated form of the substrate. A His side chain acts as back door that "pushes" the substrate-reactive carbon atom toward the N5-C4a locus of the flavin. Analysis of the three-dimensional structure reveals possible pathways for diffusion of molecular oxygen and a small cavity on the re side of the flavin that may host oxygen during FAD reoxidation. These features combined with the tight shape of the catalytic site provide insights into the mechanism of AldO-mediated regioselective oxidation reactions and its substrate specificity.
Structural Analysis of the Catalytic Mechanism and Stereoselectivity in Streptomyces coelicolor Alditol Oxidase(,).,Forneris F, Heuts DP, Delvecchio M, Rovida S, Fraaije MW, Mattevi A Biochemistry. 2008 Jan 22;47(3):978-85. Epub 2007 Dec 23. PMID:18154360[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Heuts DP, van Hellemond EW, Janssen DB, Fraaije MW. Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor. J Biol Chem. 2007 Jul 13;282(28):20283-91. PMID:17517896 doi:10.1074/jbc.M610849200
- ↑ Forneris F, Heuts DP, Delvecchio M, Rovida S, Fraaije MW, Mattevi A. Structural Analysis of the Catalytic Mechanism and Stereoselectivity in Streptomyces coelicolor Alditol Oxidase(,). Biochemistry. 2008 Jan 22;47(3):978-85. Epub 2007 Dec 23. PMID:18154360 doi:10.1021/bi701886t
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