4ni3
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4ni3 is ON HOLD Authors: Cao, H., Walton, J. D., Brumm, P., Phillips Jr., G. N. Description: Crystal Structure of GH29 family alpha-L-fucosidase fr...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of GH29 family alpha-L-fucosidase from Fusarium graminearum in the closed form== | |
| + | <StructureSection load='4ni3' size='340' side='right'caption='[[4ni3]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ni3]] 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=4NI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NI3 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]] 1.3993Å</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=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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ni3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni3 OCA], [https://pdbe.org/4ni3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ni3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ni3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ni3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/J9UN47_GIBZA J9UN47_GIBZA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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 4ni3" 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 JD]] | ||
Current revision
Crystal Structure of GH29 family alpha-L-fucosidase from Fusarium graminearum in the closed form
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