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1cz1

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EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS AT 1.85 A RESOLUTION

Structural highlights

1cz1 is a 1 chain structure with sequence from Candida albicans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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.

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:10610795^[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
↑ Cutfield SM, Davies GJ, Murshudov G, Anderson BF, Moody PC, Sullivan PA, Cutfield JF. 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. J Mol Biol. 1999 Dec 3;294(3):771-83. PMID:10610795 doi:10.1006/jmbi.1999.3287

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cz1"

@@ Line 1: / Line 1: @@
 ==EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS AT 1.85 A RESOLUTION==
-<StructureSection load='1cz1' size='340' side='right' caption='[[1cz1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='1cz1' size='340' side='right'caption='[[1cz1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cz1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11006_[[candida_stellatoidea]] Atcc 11006 [[candida stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CZ1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cz1]] 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=1CZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CZ1 FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=1cz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cz1 OCA], [https://pdbe.org/1cz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cz1 RCSB], [https://www.ebi.ac.uk/pdbsum/1cz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cz1 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cz1 OCA], [http://pdbe.org/1cz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cz1 RCSB], [http://www.ebi.ac.uk/pdbsum/1cz1 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/1cz1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/1cz1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1cz1 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Glucanase|Glucanase]]
+*[[Glucanase 3D structures|Glucanase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Glucan 1,3-beta-glucosidase]]
+[[Category: Candida albicans]]
-[[Category: Anderson, B F]]
+[[Category: Large Structures]]
-[[Category: Cutfield, J F]]
+[[Category: Anderson BF]]
-[[Category: Cutfield, S M]]
+[[Category: Cutfield JF]]
-[[Category: Davies, G J]]
+[[Category: Cutfield SM]]
-[[Category: Moody, P C.E]]
+[[Category: Davies GJ]]
-[[Category: Murshudov, G]]
+[[Category: Moody PCE]]
-[[Category: Sullivan, P A]]
+[[Category: Murshudov G]]
-[[Category: Candida albican]]
+[[Category: Sullivan PA]]
-[[Category: Exoglucanase]]
-[[Category: Glycoside hydrolase family 5]]
-[[Category: Hydrolase]]

1cz1

From Proteopedia

Current revision

EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS AT 1.85 A RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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