Download MendeleyCrystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium
Tachioka, M., Nakamura, A., Ishida, T., Igarashi, K., Samejima, M.(2017) Acta Crystallogr F Struct Biol Commun 73: 398-403
- PubMed: 28695848
- DOI: https://doi.org/10.1107/S2053230X17008093
- Primary Citation of Related Structures:
5XCY, 5XCZ - PubMed Abstract:
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 β-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.
Organizational Affiliation:
Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
