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| | <StructureSection load='2vz1' size='340' side='right'caption='[[2vz1]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='2vz1' size='340' side='right'caption='[[2vz1]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vz1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusairum_graminearum Fusairum graminearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vz1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_graminearum Fusarium graminearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZ1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.91Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t2x|1t2x]], [[1goh|1goh]], [[1gof|1gof]], [[1k3i|1k3i]], [[1gog|1gog]], [[2vz3|2vz3]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.9 1.1.3.9] </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=2vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vz1 OCA], [https://pdbe.org/2vz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vz1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vz1 ProSAT]</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=2vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vz1 OCA], [https://pdbe.org/2vz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vz1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vz1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GAOA_GIBZE GAOA_GIBZE]] Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides (By similarity).
| + | [https://www.uniprot.org/uniprot/GAOA_GIBZA GAOA_GIBZA] Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.<ref>PMID:13641238</ref> <ref>PMID:4441089</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: Fusairum graminearum]] | + | [[Category: Fusarium graminearum]] |
| - | [[Category: Galactose oxidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dooley, D M]] | + | [[Category: Dooley DM]] |
| - | [[Category: Firbank, S J]] | + | [[Category: Firbank SJ]] |
| - | [[Category: Halcrow, M A]] | + | [[Category: Halcrow MA]] |
| - | [[Category: Hurtado-Guerrero, R]] | + | [[Category: Hurtado-Guerrero R]] |
| - | [[Category: Knowles, P F]] | + | [[Category: Knowles PF]] |
| - | [[Category: McPherson, M J]] | + | [[Category: McPherson MJ]] |
| - | [[Category: Phillips, S E.V]] | + | [[Category: Phillips SEV]] |
| - | [[Category: Rogers, M S]] | + | [[Category: Rogers MS]] |
| - | [[Category: Anaerobic processing]]
| + | |
| - | [[Category: Copper]]
| + | |
| - | [[Category: Kelch repeat]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Thio-ether bond]]
| + | |
| - | [[Category: Thioether bond]]
| + | |
| Structural highlights
Function
GAOA_GIBZA Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.[1] [2]
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
Galactose oxidase (GO) belongs to a class of proteins that self-catalyze assembly of their redox-active cofactors from active site amino acids. Generation of enzymatically active GO appears to require at least four sequential post-translational modifications: cleavage of a secretion signal sequence, copper-dependent cleavage of an N-terminal pro sequence, copper-dependent formation of a C228-Y272 thioether bond, and generation of the Y272 radical. The last two processes were investigated using a truncated protein (termed premat-GO) lacking the pro sequence and purified under copper-free conditions. Reactions of premat-GO with Cu(II) were investigated using optical, EPR, and resonance Raman spectroscopy, SDS-PAGE, and X-ray crystallography. Premat-GO reacted anaerobically with excess Cu(II) to efficiently form the thioether bond but not the Y272 radical. A potential C228-copper coordinated intermediate (lambda max = 406 nm) in the processing reaction, which had not yet formed the C228-Y272 cross-link, was identified from the absorption spectrum. A copper-thiolate protein complex, with copper coordinated to C228, H496, and H581, was also observed in a 3 min anaerobic soak by X-ray crystallography, whereas a 24 h soak revealed the C228-Y272 thioether bond. In solution, addition of oxygenated buffer to premat-GO preincubated with excess Cu(II) generated the Y272 radical state. On the basis of these data, a mechanism for the formation of the C228-Y272 bond and tyrosyl radical generation is proposed. The 406 nm complex is demonstrated to be a catalytically competent processing intermediate under anaerobic conditions. We propose a potential mechanism which is in common with aerobic processing by Cu(II) until the step at which the second electron acceptor is required.
Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen.,Rogers MS, Hurtado-Guerrero R, Firbank SJ, Halcrow MA, Dooley DM, Phillips SE, Knowles PF, McPherson MJ Biochemistry. 2008 Sep 30;47(39):10428-39. Epub 2008 Sep 5. PMID:18771294[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ COOPER JA, SMITH W, BACILA M, MEDINA H. Galactose oxidase from Polyporus circinatus, Fr. J Biol Chem. 1959 Mar;234(3):445-8 PMID:13641238
- ↑ Kosman DJ, Ettinger MJ, Weiner RE, Massaro EJ. The molecular properties of the copper enzyme galactose oxidase. Arch Biochem Biophys. 1974 Dec;165(2):456-67. PMID:4441089 doi:10.1016/0003-9861(74)90271-9
- ↑ Rogers MS, Hurtado-Guerrero R, Firbank SJ, Halcrow MA, Dooley DM, Phillips SE, Knowles PF, McPherson MJ. Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen. Biochemistry. 2008 Sep 30;47(39):10428-39. Epub 2008 Sep 5. PMID:18771294 doi:http://dx.doi.org/10.1021/bi8010835
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