2pc8

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(New page: 200px {{Structure |PDB= 2pc8 |SIZE=350|CAPTION= <scene name='initialview01'>2pc8</scene>, resolution 1.800&Aring; |SITE= <scene name='pdbsite=AC1:Bgc+Binding+Site...)
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[[Image:2pc8.jpg|left|200px]]
 
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{{Structure
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==E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two separately bound glucopyranoside units at 1.8 A==
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|PDB= 2pc8 |SIZE=350|CAPTION= <scene name='initialview01'>2pc8</scene>, resolution 1.800&Aring;
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<StructureSection load='2pc8' size='340' side='right'caption='[[2pc8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Bgc+Binding+Site+For+Residue+A+401'>AC1</scene> and <scene name='pdbsite=AC2:Bgc+Binding+Site+For+Residue+A+402'>AC2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>
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<table><tr><td colspan='2'>[[2pc8]] 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=2PC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PC8 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,3-beta-glucosidase Glucan 1,3-beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.58 3.2.1.58] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE= XOG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 Candida albicans])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00150 Cellulase], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG2730 BglC]</span>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pc8 OCA], [https://pdbe.org/2pc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pc8 RCSB], [https://www.ebi.ac.uk/pdbsum/2pc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pc8 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1eqp|1EQP]], [[1eqc|1EQC]], [[2pb1|2PB1]], [[2pbo|2PBO]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pc8 OCA], [http://www.ebi.ac.uk/pdbsum/2pc8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pc8 RCSB]</span>
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== Function ==
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}}
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/2pc8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pc8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two separately bound glucopyranoside units at 1.8 A'''
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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<ref>PMID:20875088</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2pc8" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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A group of fungal exo-beta-(1,3)-glucanases, including that from the human pathogen Candida albicans (Exg), belong to glycosyl hydrolase family 5 that also includes many bacterial cellulases (endo-beta-1, 4-glucanases). Family members, despite wide sequence variations, share a common mechanism and are characterised by possessing eight invariant residues making up the active site. These include two glutamate residues acting as nucleophile and acid/base, respectively. Exg is an abundant secreted enzyme possessing both hydrolase and transferase activity consistent with a role in cell wall glucan metabolism and possibly morphogenesis. The structures of Exg in both free and inhibited forms have been determined to 1.9 A resolution. A distorted (beta/alpha)8 barrel structure accommodates an active site which is located within a deep pocket, formed when extended loop regions close off a cellulase-like groove. Structural analysis of a covalently bound mechanism-based inhibitor (2-fluoroglucosylpyranoside) and of a transition-state analogue (castanospermine) has identified the binding interactions at the -1 glucose binding site. In particular the carboxylate of Glu27 serves a dominant hydrogen-bonding role. Access by a 1,3-glucan chain to the pocket in Exg can be understood in terms of a change in conformation of the terminal glucose residue from chair to twisted boat. The geometry of the pocket is not, however, well suited for cleavage of 1,4-glycosidic linkages. A second glucose site was identified at the entrance to the pocket, sandwiched between two antiparallel phenylalanine side-chains. This aromatic entrance-way must not only direct substrate into the pocket but also may act as a clamp for an acceptor molecule participating in the transfer reaction.
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2PC8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PC8 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The structure of the exo-beta-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases., Cutfield SM, Davies GJ, Murshudov G, Anderson BF, Moody PC, Sullivan PA, Cutfield JF, J Mol Biol. 1999 Dec 3;294(3):771-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10610795 10610795]
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[[Category: Candida albicans]]
[[Category: Candida albicans]]
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[[Category: Glucan 1,3-beta-glucosidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cutfield JF]]
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[[Category: Cutfield, J F.]]
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[[Category: Cutfield SM]]
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[[Category: Cutfield, S M.]]
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[[Category: Patrick WM]]
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[[Category: Patrick, W M.]]
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[[Category: additional ch binding site]]
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[[Category: candida albican]]
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[[Category: carbohydrate binding]]
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[[Category: exo-glucanase]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 2 11:57:23 2008''
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Current revision

E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two separately bound glucopyranoside units at 1.8 A

PDB ID 2pc8

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