1WO2
Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion
Summary for 1WO2
| Entry DOI | 10.2210/pdb1wo2/pdb |
| Related | 1HX0 1UA3 |
| Related PRD ID | PRD_900018 PRD_900065 |
| Descriptor | Alpha-amylase, pancreatic, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | beta-alpha-barrels, hydrolase |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 57271.94 |
| Authors | Qian, M.,Payan, F.,Nahoum, V. (deposition date: 2004-08-11, release date: 2005-03-15, Last modification date: 2024-11-13) |
| Primary citation | Qian, M.,Ajandouz, E.H.,Payan, F.,Nahoum, V. Molecular Basis of the Effects of Chloride Ion on the Acid-Base Catalyst in the Mechanism of Pancreatic alpha-Amylase Biochemistry, 44:3194-3201, 2005 Cited by PubMed Abstract: Pig pancreatic alpha-amylase (PPA), an enzyme belonging to the alpha-amylase family, is involved in the degradation of starch. Like some other members of this family, PPA requires chloride to reach maximum activity levels. To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free buffer was analyzed by X-ray crystallography. A conspicuous reorientation of the acid/base catalyst Glu233 residue was found to occur. The structural results, along with kinetic data, show that the acid/base catalyst is maintained in the active site, in an optimum position, pointing toward the scissile bond-atom, due to the presence of chloride ions. The present study therefore explains the mechanism of PPA activation by chloride ions. PubMed: 15736930DOI: 10.1021/bi048201t PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
Download full validation report
