5XCY
Structure of the cellobiohydrolase Cel6A from Phanerochaete chrysosporium at 1.2 angstrom
Summary for 5XCY
| Entry DOI | 10.2210/pdb5xcy/pdb |
| Related | 5XCZ |
| Descriptor | Glucanase (2 entities in total) |
| Functional Keywords | glycoside hydrolase family 6, hydrolase |
| Biological source | Phanerochaete chrysosporium (White-rot fungus) |
| Total number of polymer chains | 1 |
| Total formula weight | 38381.57 |
| Authors | Tachioka, M.,Nakamura, A.,Ishida, T.,Igarashi, K.,Samejima, M. (deposition date: 2017-03-24, release date: 2017-07-26, Last modification date: 2024-11-13) |
| Primary citation | 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, 73:398-403, 2017 Cited by PubMed 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 β-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. PubMed: 28695848DOI: 10.1107/S2053230X17008093 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.199 Å) |
Structure validation
Download full validation report
