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 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 language | English |
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Pages (from-to) | 398-403 |
Journal | Acta Crystallographica Section F: Structural Biology Communications |
Volume | 73 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2017 |
MoE publication type | A1 Journal article-refereed |
Keywords
- biomass utilization
- carbohydrate-active enzymes
- cellobiohydrolase
- cellulases
- Phanerochaete chrysosporium