8z2y

From Proteopedia

(Difference between revisions)

Current revision

High-resolution crystal structure of exo-beta-(1,3)-glucanase from Aspergillus oryzae (AoBgl) as a complex with glucose

Structural highlights

8z2y is a 1 chain structure with sequence from Aspergillus oryzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.2Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EXGA_ASPOR 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 (By similarity).^[1]

Publication Abstract from PubMed

Exo-beta-(1,3)-glucanases are promising enzymes for use in the biofuel industry as they hydrolyse sugars such as laminarin, a major constituent of the algal cell wall. This study reports structural and biochemical characterizations of Aspergillus oryzae exo-beta-(1,3)-glucanase (AoBgl) belonging to the GH5 family. Purified AoBgl hydrolyses beta-(1,3)-glycosidic linkages of the oligosaccharide laminaritriose and the polysaccharide laminarin effectively. We have determined three high-resolution structures of AoBgl: (a) the apo form at 1.75 A, (b) the complexed form with bound cellobiose at 1.73 A and (c) the glucose-bound form at 1.20 A. The crystal structures, molecular dynamics simulation studies and site-directed mutagenesis reveal the mode of substrate binding and interactions at the active site. The results also indicate that AoBgl effectively hydrolyses trisaccharides and higher oligosaccharides. The findings from our structural and biochemical studies would aid in rational engineering efforts to generate superior AoBgl variants and similar GH5 enzymes for their industrial use.

Crystal structures of Aspergillus oryzae exo-beta-(1,3)-glucanase reveal insights into oligosaccharide binding, recognition, and hydrolysis.,Banerjee B, Kamale CK, Suryawanshi AB, Dasgupta S, Noronha S, Bhaumik P FEBS Lett. 2024 Oct 24. doi: 10.1002/1873-3468.15045. PMID:39448541^[2]

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

References

↑ Tamano K, Satoh Y, Ishii T, Terabayashi Y, Ohtaki S, Sano M, Takahashi T, Koyama Y, Mizutani O, Abe K, Machida M. The beta-1,3-exoglucanase gene exgA (exg1) of Aspergillus oryzae is required to catabolize extracellular glucan, and is induced in growth on a solid surface. Biosci Biotechnol Biochem. 2007 Apr;71(4):926-34. PMID:17420593 doi:10.1271/bbb.60591
↑ Banerjee B, Kamale CK, Suryawanshi AB, Dasgupta S, Noronha S, Bhaumik P. Crystal structures of Aspergillus oryzae exo-β-(1,3)-glucanase reveal insights into oligosaccharide binding, recognition, and hydrolysis. FEBS Lett. 2024 Oct 24. PMID:39448541 doi:10.1002/1873-3468.15045

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8z2y"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8z2y is ON HOLD  until Paper Publication
+==High-resolution crystal structure of exo-beta-(1,3)-glucanase from Aspergillus oryzae (AoBgl) as a complex with glucose==
+<StructureSection load='8z2y' size='340' side='right'caption='[[8z2y]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8z2y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Z2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Z2Y FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
+<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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=8z2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8z2y OCA], [https://pdbe.org/8z2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8z2y RCSB], [https://www.ebi.ac.uk/pdbsum/8z2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8z2y ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EXGA_ASPOR EXGA_ASPOR] 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 (By similarity).<ref>PMID:17420593</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Exo-beta-(1,3)-glucanases are promising enzymes for use in the biofuel industry as they hydrolyse sugars such as laminarin, a major constituent of the algal cell wall. This study reports structural and biochemical characterizations of Aspergillus oryzae exo-beta-(1,3)-glucanase (AoBgl) belonging to the GH5 family. Purified AoBgl hydrolyses beta-(1,3)-glycosidic linkages of the oligosaccharide laminaritriose and the polysaccharide laminarin effectively. We have determined three high-resolution structures of AoBgl: (a) the apo form at 1.75 A, (b) the complexed form with bound cellobiose at 1.73 A and (c) the glucose-bound form at 1.20 A. The crystal structures, molecular dynamics simulation studies and site-directed mutagenesis reveal the mode of substrate binding and interactions at the active site. The results also indicate that AoBgl effectively hydrolyses trisaccharides and higher oligosaccharides. The findings from our structural and biochemical studies would aid in rational engineering efforts to generate superior AoBgl variants and similar GH5 enzymes for their industrial use.
-Authors:
+Crystal structures of Aspergillus oryzae exo-beta-(1,3)-glucanase reveal insights into oligosaccharide binding, recognition, and hydrolysis.,Banerjee B, Kamale CK, Suryawanshi AB, Dasgupta S, Noronha S, Bhaumik P FEBS Lett. 2024 Oct 24. doi: 10.1002/1873-3468.15045. PMID:39448541<ref>PMID:39448541</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8z2y" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aspergillus oryzae]]
+[[Category: Large Structures]]
+[[Category: Banerjee B]]
+[[Category: Bhaumik P]]
+[[Category: Kamale CK]]
+[[Category: Suryawanshi AB]]

8z2y

From Proteopedia

Current revision

High-resolution crystal structure of exo-beta-(1,3)-glucanase from Aspergillus oryzae (AoBgl) as a complex with glucose

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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