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

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 ?-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.

SUBMITTER: Tachioka M

PROVIDER: S-EPMC5505244 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature

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

Tachioka Mikako M Nakamura Akihiko A Ishida Takuya T Igarashi Kiyohiko K Samejima Masahiro M

Acta crystallographica. Section F, Structural biology communications 20170617 Pt 7

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. ...[more]

PMID: 28695848

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