2pb1

From Proteopedia

(Difference between revisions)

Revision as of 15:20, 17 June 2021

Exo-B-(1,3)-Glucanase from Candida Albicans in complex with unhydrolysed and covalently linked 2,4-dinitrophenyl-2-deoxy-2-fluoro-B-D-glucopyranoside at 1.9 A

Structural highlights

2pb1 is a 1 chain structure with sequence from monilia_stellatoidea Atcc 11006 monilia stellatoidea . Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1eqp, 1eqc
Gene:	EXG (ATCC 11006 Monilia stellatoidea )
Activity:	Glucan 1,3-beta-glucosidase, with EC number 3.2.1.58
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pb1"

@@ Line 1: / Line 1: @@
 ==Exo-B-(1,3)-Glucanase from Candida Albicans in complex with unhydrolysed and covalently linked 2,4-dinitrophenyl-2-deoxy-2-fluoro-B-D-glucopyranoside at 1.9 A==
-<StructureSection load='2pb1' size='340' side='right' caption='[[2pb1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='2pb1' size='340' side='right'caption='[[2pb1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pb1]] 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=2PB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PB1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pb1]] 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=2PB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PB1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=NFG:2,4-DINITROPHENYL+2-DEOXY-2-FLUORO-BETA-D-GLUCOPYRANOSIDE'>NFG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=NFG:2,4-DINITROPHENYL+2-DEOXY-2-FLUORO-BETA-D-GLUCOPYRANOSIDE'>NFG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eqp|1eqp]], [[1eqc|1eqc]]</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]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 ATCC 11006 [[Candida stellatoidea]]])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXG ([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'>[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>
+<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pb1 OCA], [http://pdbe.org/2pb1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pb1 RCSB], [http://www.ebi.ac.uk/pdbsum/2pb1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pb1 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=2pb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pb1 OCA], [https://pdbe.org/2pb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pb1 RCSB], [https://www.ebi.ac.uk/pdbsum/2pb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pb1 ProSAT]</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/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.
 == 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/pb/2pb1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pb/2pb1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Glucan 1,3-beta-glucosidase]]
+[[Category: Large Structures]]
 [[Category: Cutfield, J F]]
 [[Category: Cutfield, S M]]

2pb1

From Proteopedia

Revision as of 15:20, 17 June 2021

Exo-B-(1,3)-Glucanase from Candida Albicans in complex with unhydrolysed and covalently linked 2,4-dinitrophenyl-2-deoxy-2-fluoro-B-D-glucopyranoside at 1.9 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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