1BLI
BACILLUS LICHENIFORMIS ALPHA-AMYLASE
Summary for 1BLI
| Entry DOI | 10.2210/pdb1bli/pdb |
| Descriptor | ALPHA-AMYLASE, CALCIUM ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, glycosyltransferase, alpha-amylase, starch degradation, alpha-1, 4-glucan-4-glucanohydrolase, thermostability, calcium, sodium |
| Biological source | Bacillus licheniformis |
| Total number of polymer chains | 1 |
| Total formula weight | 55410.18 |
| Authors | Machius, M.,Declerck, N.,Huber, R.,Wiegand, G. (deposition date: 1998-01-07, release date: 1999-03-23, Last modification date: 2024-05-22) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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