This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4psr
From Proteopedia
(Difference between revisions)
(New page: {{STRUCTURE_4psr| PDB=4psr | SCENE= }} ===Crystal Structure of alpha-L-fucosidase from Fusarium graminearum in the open form in complex with L-fucose=== ==About this Structure== [[4p...) |
|||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_4psr| PDB=4psr | SCENE= }} | ||
| - | ===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== |
| - | [[4psr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSR OCA]. | + | <StructureSection load='4psr' size='340' side='right'caption='[[4psr]], [[Resolution|resolution]] 1.38Å' scene=''> |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38Å</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> |
| - | [[Category: | + | <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> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/J9UN47_GIBZA J9UN47_GIBZA] |
| - | [[Category: | + | <div style="background-color:#fffaf0;"> |
| - | [[Category: | + | == 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<ref>PMID:25086049</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4psr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Fusarium graminearum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brumm P]] | ||
| + | [[Category: Cao H]] | ||
| + | [[Category: Phillips Jr GN]] | ||
| + | [[Category: Walton J]] | ||
Current revision
Crystal Structure of alpha-L-fucosidase from Fusarium graminearum in the open form in complex with L-fucose
| |||||||||||
