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| | <StructureSection load='2pf0' size='340' side='right'caption='[[2pf0]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2pf0' size='340' side='right'caption='[[2pf0]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2pf0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11006_[[monilia_stellatoidea]] Atcc 11006 [[monilia stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PF0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2pf0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PF0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eqp|1eqp]], [[1eqc|1eqc]], [[2pb1|2pb1]], [[2pc8|2pc8]], [[2pbo|2pbo]]</div></td></tr> | + | </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=2pf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pf0 OCA], [https://pdbe.org/2pf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pf0 RCSB], [https://www.ebi.ac.uk/pdbsum/2pf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pf0 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XOG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 ATCC 11006 [[Monilia stellatoidea]]])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucan_1,3-beta-glucosidase Glucan 1,3-beta-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.58 3.2.1.58] </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=2pf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pf0 OCA], [https://pdbe.org/2pf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pf0 RCSB], [https://www.ebi.ac.uk/pdbsum/2pf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pf0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/EXG_CANAL EXG_CANAL]] Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase.
| + | [https://www.uniprot.org/uniprot/EXG1_CANAL EXG1_CANAL] Major glucan 1,3-beta-glucosidase required for cell wall integrity. Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Can also function biosynthetically as a transglycosylase. Functions to deliver glucan from the cell to the extracellular matrix. Does not appear to impact cell wall glucan content of biofilm cells, nor is it necessary for filamentation or biofilm formation. Involved in cell-substrate and cell-cell adhesion. Adhesion to host-cell surfaces is the first critical step during mucosal infection. XOG1 is target of human antimicrobial peptide LL-37 for inhibition of cell adhesion.<ref>PMID:21713010</ref> <ref>PMID:22876186</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: Glucan 1,3-beta-glucosidase]] | + | [[Category: Candida albicans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cutfield, J F]] | + | [[Category: Cutfield JF]] |
| - | [[Category: Cutfield, S M]] | + | [[Category: Cutfield SM]] |
| - | [[Category: Patrick, W M]] | + | [[Category: Patrick WM]] |
| - | [[Category: Aromatic entranceway]]
| + | |
| - | [[Category: Candida albican]]
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| - | [[Category: Carbohydrate binding]]
| + | |
| - | [[Category: Exo-glucanase]]
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| - | [[Category: Hydrolase]]
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| Structural highlights
Function
EXG1_CANAL Major glucan 1,3-beta-glucosidase required for cell wall integrity. Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Can also function biosynthetically as a transglycosylase. Functions to deliver glucan from the cell to the extracellular matrix. Does not appear to impact cell wall glucan content of biofilm cells, nor is it necessary for filamentation or biofilm formation. Involved in cell-substrate and cell-cell adhesion. Adhesion to host-cell surfaces is the first critical step during mucosal infection. XOG1 is target of human antimicrobial peptide LL-37 for inhibition of cell adhesion.[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
Candida albicans exo-beta-1,3-glucanase (Exg; EC 3.2.1.58) is implicated in cell wall beta-d-glucan remodelling through its glucosyl hydrolase and/or transglucosylase activities. A pair of antiparallel phenylalanyl residues (F144 and F258) flank the entrance to the active site pocket. Various Exg mutants were studied using steady-state kinetics and crystallography aiming to understand the roles played by these residues in positioning the beta-1,3-d-glucan substrate. Mutations at the Phe-Phe entranceway demonstrated the requirement for double-sided CH/pi interactions at the +1 subsite, and the necessity for phenylalanine rather than tyrosine or tryptophan. The Tyr-Tyr double mutations introduced ordered water molecules into the entranceway. A third Phe residue (F229) nearby was evaluated as a possible +2 subsite. The inactive double mutant E292S/F229A complexed with laminaritriose has provided the first picture of substrate binding to Exg and demonstrated how the Phe-Phe arrangement acts as a clamp at the +1 subsite. The terminal sugar at the -1 site showed displacement from the position of a monosaccharide analogue with interchange of water molecules and sugar hydroxyls. An unexpected additional glucose binding site, well removed from the active site, was revealed. This site may enable Exg to associate with the branched glucan structure of the C. albicans cell wall.
Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance.,Patrick WM, Nakatani Y, Cutfield SM, Sharpe ML, Ramsay RJ, Cutfield JF FEBS J. 2010 Sep 10. doi: 10.1111/j.1742-4658.2010.07869.x. PMID:20875088[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tsai PW, Yang CY, Chang HT, Lan CY. Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37. PLoS One. 2011;6(6):e21394. doi: 10.1371/journal.pone.0021394. Epub 2011 Jun 21. PMID:21713010 doi:http://dx.doi.org/10.1371/journal.pone.0021394
- ↑ Taff HT, Nett JE, Zarnowski R, Ross KM, Sanchez H, Cain MT, Hamaker J, Mitchell AP, Andes DR. A Candida biofilm-induced pathway for matrix glucan delivery: implications for drug resistance. PLoS Pathog. 2012;8(8):e1002848. doi: 10.1371/journal.ppat.1002848. Epub 2012 Aug, 2. PMID:22876186 doi:http://dx.doi.org/10.1371/journal.ppat.1002848
- ↑ Patrick WM, Nakatani Y, Cutfield SM, Sharpe ML, Ramsay RJ, Cutfield JF. Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance. FEBS J. 2010 Sep 10. doi: 10.1111/j.1742-4658.2010.07869.x. PMID:20875088 doi:10.1111/j.1742-4658.2010.07869.x
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