1DKP
CRYSTAL STRUCTURE OF PHYTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS AS AN INTERMOLECULAR BRIDGE
Summary for 1DKP
| Entry DOI | 10.2210/pdb1dkp/pdb |
| Related | 1DKL 1DKM 1DKN 1DKO 1DKQ |
| Descriptor | PHYTASE, MERCURY (II) ION, INOSITOL HEXAKISPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | histidine acid phosphatase fold, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 46159.00 |
| Authors | Lim, D.,Golovan, S.,Forsberg, C.W.,Jia, Z. (deposition date: 1999-12-08, release date: 2000-08-03, Last modification date: 2024-10-30) |
| Primary citation | Lim, D.,Golovan, S.,Forsberg, C.W.,Jia, Z. Crystal structures of Escherichia coli phytase and its complex with phytate. Nat.Struct.Biol., 7:108-113, 2000 Cited by PubMed Abstract: Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of E. coli phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of E. coli phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid. PubMed: 10655611DOI: 10.1038/72371 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
Download full validation report
