Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 398-403 |
| Number of pages | 6 |
| 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 |
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Keywords
- biomass utilization
- carbohydrate-active enzymes
- cellobiohydrolase
- cellulases
- Phanerochaete chrysosporium
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Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium. / Tachioka, Mikako; Nakamura, Akihiko; Ishida, Takuya; Igarashi, Kiyohiko; Samejima, Masahiro.
In: Acta Crystallographica Section F: Structural Biology Communications, Vol. 73, No. 7, 2017, p. 398-403.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium
AU - Tachioka, Mikako
AU - Nakamura, Akihiko
AU - Ishida, Takuya
AU - Igarashi, Kiyohiko
AU - Samejima, Masahiro
PY - 2017
Y1 - 2017
N2 - 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.
AB - 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.
KW - biomass utilization
KW - carbohydrate-active enzymes
KW - cellobiohydrolase
KW - cellulases
KW - Phanerochaete chrysosporium
UR - http://www.scopus.com/inward/record.url?scp=85023206345&partnerID=8YFLogxK
U2 - 10.1107/S2053230X17008093
DO - 10.1107/S2053230X17008093
M3 - Article
VL - 73
SP - 398
EP - 403
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
IS - 7
ER -