3atg

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3atg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulosimicrobium_cellulans Cellulosimicrobium cellulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ATG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ATG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3atg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulosimicrobium_cellulans Cellulosimicrobium cellulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ATG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ATG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 1.66&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucan_endo-1,3-beta-D-glucosidase Glucan endo-1,3-beta-D-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.39 3.2.1.39] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3atg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atg OCA], [https://pdbe.org/3atg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3atg RCSB], [https://www.ebi.ac.uk/pdbsum/3atg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3atg 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=3atg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atg OCA], [https://pdbe.org/3atg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3atg RCSB], [https://www.ebi.ac.uk/pdbsum/3atg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3atg ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G1ED17_CELCE G1ED17_CELCE]
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Endo-1,3-beta-glucanase from Cellulosimicrobium cellulans is composed of a catalytic domain and a carbohydrate-binding module. We have determined the X-ray crystal structure of the catalytic domain at a high resolution of 1.66A. The overall fold is a sandwich-like beta-jelly roll architecture like the enzymes in the glycoside hydrolase family 16. The substrate-binding cleft has a length and a width of ~28 and ~15A, respectively, which is thought to be capable of accommodating at least six glucopyranose units. Laminarihexaose was placed into the substrate-binding cleft, namely at the subsites +2 to -4 from the reducing end, and the complex structure was analyzed using molecular dynamics simulations (MD) and using a rotamer search of the pocket. During the MD simulations, the substrate fluctuated more than the enzyme, where the residues at the subsites toward the non-reducing end fluctuated more than those toward the reducing end. Little conformational change of the protein was observed for the subsites +1 and +2, indicating that the glucose's position could be tightly restricted inside the pocket. Substrate binding experiments using isothermal titration calorimetry showed that the binding affinity of laminaritriose was higher than that of laminaribiose and similar to those of other longer laminarioligosaccharides. Taken together, the substrates mainly bind to the subsites -1 to -3 with the highest affinity, while the part bound to the reducing end would be hydrolyzed.
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Structural and thermodynamic characterization of endo-1,3-beta-glucanase: Insights into the substrate recognition mechanism.,Oda M, Inaba S, Kamiya N, Bekker GJ, Mikami B Biochim Biophys Acta. 2017 Dec 12;1866(3):415-425. doi:, 10.1016/j.bbapap.2017.12.004. PMID:29246508<ref>PMID:29246508</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 3atg" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glucanase|Glucanase]]
*[[Glucanase|Glucanase]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cellulosimicrobium cellulans]]
[[Category: Cellulosimicrobium cellulans]]
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[[Category: Glucan endo-1,3-beta-D-glucosidase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mikami, B]]
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[[Category: Mikami B]]
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[[Category: Oda, M]]
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[[Category: Oda M]]
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[[Category: Pang, Z]]
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[[Category: Pang Z]]
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[[Category: Tanabe, Y]]
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[[Category: Tanabe Y]]
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[[Category: Beta-sandwich fold]]
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[[Category: Carbohydrate/sugar binding]]
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[[Category: Hydrolase]]
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Current revision

endo-1,3-beta-glucanase from Cellulosimicrobium cellulans

PDB ID 3atg

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