5h9x

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Current revision (09:15, 20 March 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A1S4NYE1_9BACL A0A1S4NYE1_9BACL]
[https://www.uniprot.org/uniprot/A0A1S4NYE1_9BACL A0A1S4NYE1_9BACL]
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== Publication Abstract from PubMed ==
 
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beta-1,3-Glucan is one of the most abundant polysaccharides in fungi. Recognition of beta-1,3-glucan occurs in both hydrolysis by glycoside hydrolases and immunological recognition. Our study provides a novel structural account of how glycoside hydrolase recognizes and hydrolyzes substrates in a triple-helical form and presents a general structural basis of beta-1,3-glucan recognition.
 
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The recognition mechanism of triple-helical beta-1,3-glucan by a beta-1,3-glucanase.,Qin Z, Yang D, You X, Liu Y, Hu S, Yan Q, Yang S, Jiang Z Chem Commun (Camb). 2017 Aug 17;53(67):9368-9371. doi: 10.1039/c7cc03330c. PMID:28787048<ref>PMID:28787048</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 class="pdbe-citations 5h9x" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
 
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<references/>
 
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</StructureSection>
</StructureSection>

Current revision

Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii

PDB ID 5h9x

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