8WUP
X-Ray crystal structure of glycoside hydrolase family 6 cellobiohydrolase from Phanerochaete chrysosporium PcCel6A wild-type
Summary for 8WUP
| Entry DOI | 10.2210/pdb8wup/pdb |
| Descriptor | Glucanase (2 entities in total) |
| Functional Keywords | glycoside hydrolase family 6, cellobiohydrolase, cellulase, wild-type catalytic domain, hydrolase |
| Biological source | Phanerodontia chrysosporium |
| Total number of polymer chains | 1 |
| Total formula weight | 38381.57 |
| Authors | Yamaguchi, S.,Sunagawa, N.,Tachioka, M.,Igarashi, K. (deposition date: 2023-10-20, release date: 2024-09-04, Last modification date: 2024-10-16) |
| Primary citation | Yamaguchi, S.,Sunagawa, N.,Samejima, M.,Igarashi, K. Thermotolerance Mechanism of Fungal GH6 Cellobiohydrolase. Part II. Structural Analysis of Thermotolerant Mutant from the Basidiomycete Phanerochaete chrysosporium. J Appl Glycosci (1999), 71:63-72, 2024 Cited by PubMed Abstract: 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 (Cel6A) by replacing the two free cysteine (Cys) residues, C240 and C393, with serine (Yamaguchi ., J Appl Glycosci. 2020; 67;79-86). In the accompanying paper (Part I; Yamaguchi ., 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 -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. PubMed: 38863950DOI: 10.5458/jag.jag.JAG-2023_0018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.99 Å) |
Structure validation
Download full validation report
