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==X-Ray crystal structure of glycoside hydrolase family 6 cellobiohydrolase from Phanerochaete chrysosporium PcCel6A wild-type==
<StructureSection load='8wup' size='340' side='right'caption='[[8wup]], [[Resolution|resolution]] 0.99&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8wup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WUP 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]] 0.99&#8491;</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=8wup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wup OCA], [https://pdbe.org/8wup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wup RCSB], [https://www.ebi.ac.uk/pdbsum/8wup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wup ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H3K419_PHACH H3K419_PHACH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoside hydrolase family 6 cellobiohydrolase (GH6 CBH) is a group of cellulases capable of hydrolyzing crystalline cellulose. However, the synergistic reaction of GH6 CBH with other cellulases is hindered by its relatively low thermotolerance. We previously obtained a thermotolerant double mutant, C240S/C393S, of GH6 CBH from the basidiomycete Phanerochaete chrysosporium (PcCel6A) by replacing the two free cysteine (Cys) residues, C240 and C393, with serine (Yamaguchi et al., J Appl Glycosci. 2020; 67;79-86). In the accompanying paper (Part I; Yamaguchi et al., J Appl Glycosci. 2024; 71: 55-62), we measured the temperature dependence of the activity and folding of C240S/C393S and its single mutants, C240S and C393S, and found that replacement of C393 was the major contributor to the increased thermotolerance of C240S/C393S. Here, in order to investigate the mechanism involved, we crystallized the wild-type and the mutant enzymes and compared their X-ray crystal structures. The overall structures of the wild-type and the three mutant enzymes were similar. However, C240S/C393S had the lowest relative B-factor at both the N-terminal loop (residues 172-177) and the C-terminal loop (residues 390-425). This result suggests that reduced structural fluctuation of the substrate-enclosing loops, possibly due to stronger hydrogen bonding involving C393, could account for the increased thermotolerance of C240S/C393S.

Thermotolerance Mechanism of Fungal GH6 Cellobiohydrolase. Part II. Structural Analysis of Thermotolerant Mutant from the Basidiomycete Phanerochaete chrysosporium.,Yamaguchi S, Sunagawa N, Samejima M, Igarashi K J Appl Glycosci (1999). 2024 May 20;71(2):63-72. doi: , 10.5458/jag.jag.JAG-2023_0018. eCollection 2024. PMID:38863950<ref>PMID:38863950</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8wup" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phanerodontia chrysosporium]]
[[Category: Igarashi K]]
[[Category: Sunagawa N]]
[[Category: Tachioka M]]
[[Category: Yamaguchi S]]