3REN
CPF_2247, a novel alpha-amylase from Clostridium perfringens
Summary for 3REN
| Entry DOI | 10.2210/pdb3ren/pdb |
| Descriptor | Glycosyl hydrolase, family 8, MAGNESIUM ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | (alpha/alpha)6-barrel fold, alpha-amylase, hydrolase |
| Biological source | Clostridium perfringens |
| Total number of polymer chains | 2 |
| Total formula weight | 82300.57 |
| Authors | Ficko-Blean, E.,Stuart, C.P.,Boraston, A.B. (deposition date: 2011-04-04, release date: 2011-05-18, Last modification date: 2024-11-06) |
| Primary citation | Ficko-Blean, E.,Stuart, C.P.,Boraston, A.B. Structural analysis of CPF_2247, a novel alpha-amylase from Clostridium perfringens. Proteins, 79:2771-2777, 2011 Cited by PubMed Abstract: CPF_2247 from Clostridium perfringens ATCC 13124 was identified as a putative carbohydrate-active enzyme by its low sequence identity to endo-β-1,4-glucanases belonging to family 8 of the glycoside hydrolase classification. The X-ray crystal structure of CPF_2247 determined to 2.0 Å resolution by single-wavelength anomalous dispersion using seleno-methionine-substituted protein revealed an (α/α)(6) barrel fold. A large cleft on the surface of the protein contains residues that are structurally conserved with key elements of the catalytic machinery in clan GH-M glycoside hydrolases. Assessment of CPF_2247 as a carbohydrate-active enzyme disclosed α-glucanase activity on amylose, glycogen, and malto-oligosaccharides. PubMed: 21905105DOI: 10.1002/prot.23116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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