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

Mikako Tachioka, Akihiko Nakamura, Takuya Ishida, Kiyohiko Igarashi, Masahiro Samejima

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)398-403
Number of pages6
JournalActa Crystallographica Section F: Structural Biology Communications
Volume73
Issue number7
DOIs
Publication statusPublished - 2017
MoE publication typeA1 Journal article-refereed

Keywords

  • biomass utilization
  • carbohydrate-active enzymes
  • cellobiohydrolase
  • cellulases
  • Phanerochaete chrysosporium

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