3REN

CPF_2247, a novel alpha-amylase from Clostridium perfringens

3REN の概要

• エントリーDOI: 10.2210/pdb3ren/pdb
• 分子名称: Glycosyl hydrolase, family 8, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: (alpha/alpha)6-barrel fold, alpha-amylase, hydrolase
• 由来する生物種: Clostridium perfringens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82300.57

構造登録者

Ficko-Blean, E.,Stuart, C.P.,Boraston, A.B. (登録日: 2011-04-04, 公開日: 2011-05-18, 最終更新日: 2024-11-06)

主引用文献

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

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: 21905105
DOI: 10.1002/prot.23116

実験手法

X-RAY DIFFRACTION (2 Å)