4ni3: Difference between revisions
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== Structural highlights == | == 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> | <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='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> | </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> | <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> | </table> | ||
Latest revision as of 19:57, 20 September 2023
Crystal Structure of GH29 family alpha-L-fucosidase from Fusarium graminearum in the closed formCrystal Structure of GH29 family alpha-L-fucosidase from Fusarium graminearum in the closed form
Structural highlights
FunctionPublication Abstract from PubMedThe 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
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