1EW2
CRYSTAL STRUCTURE OF A HUMAN PHOSPHATASE
Summary for 1EW2
| Entry DOI | 10.2210/pdb1ew2/pdb |
| Descriptor | PHOSPHATASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total) |
| Functional Keywords | phosphatase, non covalent complex, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor: P05187 |
| Total number of polymer chains | 1 |
| Total formula weight | 56151.11 |
| Authors | Le Du, M.H.,Stigbrand, T.,Taussig, M.J.,Menez, A.,Stura, E.A. (deposition date: 2000-04-21, release date: 2001-04-04, Last modification date: 2020-07-29) |
| Primary citation | Le Du, M.H.,Stigbrand, T.,Taussig, M.J.,Menez, A.,Stura, E.A. Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity. J.Biol.Chem., 276:9158-9165, 2001 Cited by PubMed Abstract: Human placental alkaline phosphatase (PLAP) is one of three tissue-specific human APs extensively studied because of its ectopic expression in tumors. The crystal structure, determined at 1.8-A resolution, reveals that during evolution, only the overall features of the enzyme have been conserved with respect to Escherichia coli. The surface is deeply mutated with 8% residues in common, and in the active site, only residues strictly necessary to perform the catalysis have been preserved. Additional structural elements aid an understanding of the allosteric property that is specific for the mammalian enzyme (Hoylaerts, M. F., Manes, T., and Millán, J. L. (1997) J. Biol. Chem. 272, 22781-22787). Allostery is probably favored by the quality of the dimer interface, by a long N-terminal alpha-helix from one monomer that embraces the other one, and similarly by the exchange of a residue from one monomer in the active site of the other. In the neighborhood of the catalytic serine, the orientation of Glu-429, a residue unique to PLAP, and the presence of a hydrophobic pocket close to the phosphate product, account for the specific uncompetitive inhibition of PLAP by l-amino acids, consistent with the acquisition of substrate specificity. The location of the active site at the bottom of a large valley flanked by an interfacial crown-shaped domain and a domain containing an extra metal ion on the other side suggest that the substrate of PLAP could be a specific phosphorylated protein. PubMed: 11124260DOI: 10.1074/jbc.M009250200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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