Structural highlights
Publication Abstract from PubMed
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 beta-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.
Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.,Tachioka M, Nakamura A, Ishida T, Igarashi K, Samejima M Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):398-403. doi:, 10.1107/S2053230X17008093. Epub 2017 Jun 17. PMID:28695848[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tachioka M, Nakamura A, Ishida T, Igarashi K, Samejima M. Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium. Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):398-403. doi:, 10.1107/S2053230X17008093. Epub 2017 Jun 17. PMID:28695848 doi:http://dx.doi.org/10.1107/S2053230X17008093
