1HT6
CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1
Summary for 1HT6
| Entry DOI | 10.2210/pdb1ht6/pdb |
| Related | 1AMY |
| Descriptor | ALPHA-AMYLASE ISOZYME 1, CALCIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | barley, alpha-amylase, isozyme 1, beta-alpha-barrel, hydrolase |
| Biological source | Hordeum vulgare |
| Cellular location | Secreted, extracellular space: P00693 |
| Total number of polymer chains | 1 |
| Total formula weight | 45318.90 |
| Authors | Robert, X.,Haser, R.,Aghajari, N. (deposition date: 2000-12-29, release date: 2003-07-08, Last modification date: 2024-04-03) |
| Primary citation | Robert, X.,Haser, R.,Gottschalk, T.E.,Ratajczak, F.,Driguez, H.,Svensson, B.,Aghajari, N. The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs Structure, 11:973-984, 2003 Cited by PubMed Abstract: Though the three-dimensional structures of barley alpha-amylase isozymes AMY1 and AMY2 are very similar, they differ remarkably from each other in their affinity for Ca(2+) and when interacting with substrate analogs. A surface site recognizing maltooligosaccharides, not earlier reported for other alpha-amylases and probably associated with the different activity of AMY1 and AMY2 toward starch granules, has been identified. It is located in the C-terminal part of the enzyme and, thus, highlights a potential role of domain C. In order to scrutinize the possible biological significance of this domain in alpha-amylases, a thorough comparison of their three-dimensional structures was conducted. An additional role for an earlier-identified starch granule binding surface site is proposed, and a new calcium ion is reported. PubMed: 12906828DOI: 10.1016/S0969-2126(03)00151-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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