1BLI
BACILLUS LICHENIFORMIS ALPHA-AMYLASE
1BLI の概要
| エントリーDOI | 10.2210/pdb1bli/pdb |
| 分子名称 | ALPHA-AMYLASE, CALCIUM ION, SODIUM ION, ... (4 entities in total) |
| 機能のキーワード | hydrolase, glycosyltransferase, alpha-amylase, starch degradation, alpha-1, 4-glucan-4-glucanohydrolase, thermostability, calcium, sodium |
| 由来する生物種 | Bacillus licheniformis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 55410.18 |
| 構造登録者 | Machius, M.,Declerck, N.,Huber, R.,Wiegand, G. (登録日: 1998-01-07, 公開日: 1999-03-23, 最終更新日: 2024-05-22) |
| 主引用文献 | Machius, M.,Declerck, N.,Huber, R.,Wiegand, G. Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure, 6:281-292, 1998 Cited by PubMed Abstract: The structural basis as to how metals regulate the functional state of a protein by altering or stabilizing its conformation has been characterized in relatively few cases because the metal-free form of the protein is often partially disordered and unsuitable for crystallographic analysis. This is not the case, however, for Bacillus licheniformis alpha-amylase (BLA) for which the structure of the metal-free form is available. BLA is a hyperthermostable enzyme which is widely used in biotechnology, for example in the breakdown of starch or as a component of detergents. The determination of the structure of BLA in the metal-containing form, together with comparisons to the apo enzyme, will help us to understand the way in which metal ions can regulate enzyme activity. PubMed: 9551551DOI: 10.1016/S0969-2126(98)00032-X 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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