1VIW
TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX
Summary for 1VIW
| Entry DOI | 10.2210/pdb1viw/pdb |
| Descriptor | ALPHA-AMYLASE, ALPHA-AMYLASE-INHIBITOR, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | complex (glycosidase-inhibitor), hydrolase, lectin, insect alpha-amylase, inhibitors, complex (glycosidase-inhibitor) complex, complex (glycosidase/inhibitor) |
| Biological source | Tenebrio molitor (yellow mealworm) More |
| Total number of polymer chains | 2 |
| Total formula weight | 74872.06 |
| Authors | Nahoum, V.,Egloff, M.P.,Payan, F. (deposition date: 1998-07-21, release date: 1999-07-22, Last modification date: 2024-10-30) |
| Primary citation | Nahoum, V.,Farisei, F.,Le-Berre-Anton, V.,Egloff, M.P.,Rouge, P.,Poerio, E.,Payan, F. A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor. Acta Crystallogr.,Sect.D, 55:360-362, 1999 Cited by PubMed Abstract: The alpha-amylase from Tenebrio molitor larvae (TMA) has been crystallized in complex with the alpha-amylase inhibitor (alpha-AI) from the bean Phaseolus vulgaris. A molecular-replacement solution of the structure was obtained using the refined pig pancreatic alpha-amylase (PPA) and alpha-AI atomic coordinates as starting models. The structural analysis showed that although TMA has the typical structure common to alpha-amylases, large deviations from the mammalian alpha-amylase models occur in the loops. Despite these differences in the interacting loops, the bean inhibitor is still able to inhibit both the insect and mammalian alpha-amylase. PubMed: 10089450DOI: 10.1107/S0907444998010701 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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