Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium

Mikako Tachioka, Akihiko Nakamura, Takuya Ishida, Kiyohiko Igarashi, Masahiro Samejima

    Research output: Contribution to journalArticleScientificpeer-review

    6 Citations (Scopus)


    Cellobiohydrolases belonging to glycoside hydrolase family 6 (CBH II, Cel6A) play key roles in the hydrolysis of crystalline cellulose. CBH II from the white-rot fungus Phanerochaete chrysosporium (PcCel6A) consists of a catalytic domain (CD) and a carbohydrate-binding module connected by a linker peptide, like other known fungal cellobiohydrolases. In the present study, the CD of PcCel6A was crystallized without ligands, and p-nitrophenyl ß-d-cellotrioside (pNPG3) was soaked into the crystals. The determined structures of the ligand-free and pNPG3-soaked crystals revealed that binding of cellobiose at substrate subsites +1 and +2 induces a conformational change of the N-terminal and C-terminal loops, switching the tunnel-shaped active site from the open to the closed form.The crystal structure of the catalytic domain of a glycoside hydrolase family 6 cellobiohydrolase from the basidiomycete P. chrysosporium was solved in apo and cellobiose-liganded forms at 1.2 and 2.1 Å resolution, respectively.
    Original languageEnglish
    Pages (from-to)398-403
    JournalActa Crystallographica Section F: Structural Biology Communications
    Issue number7
    Publication statusPublished - 2017
    MoE publication typeA1 Journal article-refereed


    • biomass utilization
    • carbohydrate-active enzymes
    • cellobiohydrolase
    • cellulases
    • Phanerochaete chrysosporium


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