Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium. Issue 7 (1st July 2017)

• Record Type: Journal Article
• Authors: Tachioka, Mikako; Nakamura, Akihiko; Ishida, Takuya; Igarashi, Kiyohiko; Samejima, Masahiro
• Is Part Of: Acta crystallographica. Volume 73:Issue 7(2017:Jul.)
• Page Start: 398
• Page End: 403
• Publication Date: 2017-07-01
• Subjects: cellulases -- Phanerochaete chrysosporium -- cellobiohydrolase -- biomass utilization -- carbohydrate‐active enzymes; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X17008093
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : 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. 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 ( Pc Cel6A) 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 Pc Cel6A was crystallized without ligands, and p ‐nitrophenyl β‐d ‐cellotrioside ( p NPG3) was soaked into the crystals. The determined structures of the ligand‐free and p NPG3‐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.