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| | ==Crystal Structure of alpha-L-fucosidase from Fusarium graminearum in the open form in complex with L-fucose== | | ==Crystal Structure of alpha-L-fucosidase from Fusarium graminearum in the open form in complex with L-fucose== |
| - | <StructureSection load='4psr' size='340' side='right' caption='[[4psr]], [[Resolution|resolution]] 1.38Å' scene=''> | + | <StructureSection load='4psr' size='340' side='right'caption='[[4psr]], [[Resolution|resolution]] 1.38Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4psr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fusarium_graminarium Fusarium graminarium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PSR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4psr]] is a 2 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=4PSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PSR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ni3|4ni3]], [[4psp|4psp]], [[3eub|3eub]], [[3nvw|3nvw]], [[3nvy|3nvy]], [[3nvz|3nvz]]</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=4psr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psr OCA], [https://pdbe.org/4psr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4psr RCSB], [https://www.ebi.ac.uk/pdbsum/4psr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4psr ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5518 Fusarium graminarium])</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=4psr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psr OCA], [http://pdbe.org/4psr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4psr RCSB], [http://www.ebi.ac.uk/pdbsum/4psr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4psr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/J9UN47_GIBZA J9UN47_GIBZA] |
| | <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: Fusarium graminarium]] | + | [[Category: Fusarium graminearum]] |
| - | [[Category: Brumm, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Cao, H]] | + | [[Category: Brumm P]] |
| - | [[Category: Phillips, G N]] | + | [[Category: Cao H]] |
| - | [[Category: Walton, J]] | + | [[Category: Phillips Jr GN]] |
| - | [[Category: Fucosidase]]
| + | [[Category: Walton J]] |
| - | [[Category: Gh29]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: N-glycosylation]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
4psr is a 2 chain structure with sequence from Fusarium graminearum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
J9UN47_GIBZA
Publication Abstract from PubMed
The secreted glycoside hydrolase family 29 (GH29) alpha-L-fucosidase from plant pathogenic fungus Fusarium graminearum (FgFCO1) actively releases fucose from xyloglucan fragment. We solved crystal structures of two active-site conformations, ie., open and closed, of apo FgFCO1 and an open complex with product fucose at atomic resolution. The closed conformation supports catalysis by orienting the conserved general acid/base Glu 288 nearest the predicted glycosidic position, whereas the open conformation possibly represents an unreactive state with Glu 288 positioned away from the catalytic center. A flexible loop near the substrate binding site containing a non-conserved GGSFT sequence is ordered in the closed but not the open form. We also identified a novel C-terminal betagamma-crystallin domain in FgFCO1 devoid of calcium binding motif whose homologous sequences are present in various glycoside hydrolase families. N-glycosylated FgFCO1 adopts a monomeric state as verified by solution small angle X-ray scattering in contrast to reported multimeric fucosidases. Steady-state kinetics shows that FgFCO1 prefers alpha1,2 over alpha1,3/4-linkages and displays minimal activity with pNP-fucoside with an acidic pH optimum of 4.6. Despite a retaining GH29 family fold, the overall specificity of FgFCO1 most closely resembles inverting GH95 alpha-fucosidase which displays highest specificty with two natural substrates harboring Fucalpha1-2Gal glycosidic linkage, a xyloglucan-derived nonasaccharide and 2(prime)-fucosyllactose. Furthermore, FgFCO1 hydrolyzes H-disaccharide (lacking a +2 subsite sugar) at a rate 103-fold slower than 2(prime)-fucosyllactose. We demonstrated the structurally dynamic active site of FgFCO1 with flexible general acid/base Glu, a common feature shared by several bacterial GH29 fucosidases to various extents.
Structure and substrate specificity of a eukaryotic fucosidase from Fusarium graminearum.,Cao H, Walton JD, Brumm P, Phillips GN Jr J Biol Chem. 2014 Aug 1. pii: jbc.M114.583286. PMID:25086049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cao H, Walton JD, Brumm P, Phillips GN Jr. Structure and substrate specificity of a eukaryotic fucosidase from Fusarium graminearum. J Biol Chem. 2014 Aug 1. pii: jbc.M114.583286. PMID:25086049 doi:http://dx.doi.org/10.1074/jbc.M114.583286
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