4B6J
Crystal structure of phosphoserine phosphatase from T. onnurineus
Summary for 4B6J
| Entry DOI | 10.2210/pdb4b6j/pdb |
| Related | 4AP9 |
| Descriptor | PHOSPHOSERINE PHOSPHATASE (1 entity in total) |
| Functional Keywords | hydrolase, l-serine, haloacid dehalogenase superfamily |
| Biological source | THERMOCOCCUS ONNURINEUS NA1 |
| Total number of polymer chains | 4 |
| Total formula weight | 92074.58 |
| Authors | Jung, T.-Y.,Kim, Y.-S.,Song, H.-N.,Woo, E. (deposition date: 2012-08-14, release date: 2012-12-26, Last modification date: 2023-12-20) |
| Primary citation | Jung, T.-Y.,S-Kim, Y.,Oh, B.H.,Woo, E. Identification of a Novel Ligand Binding Site in Phosphoserine Phosphatase from the Hyperthermophilic Archaeon Thermococcus Onnurineus. Proteins, 81:819-, 2013 Cited by PubMed Abstract: Phosphoserine phosphatase (PSP) catalyzes the final and irreversible step of L-serine synthesis by hydrolyzing phosphoserine to produce L-serine and inorganic phosphate. Developing a therapeutic drug that interferes with serine production is of great interest to regulate the pathogenicity of some bacteria and control D-serine levels in neurological diseases. We determined the crystal structure of PSP from the hyperthermophilic archaeon Thermococcus onnurineus at 1.8 Å resolution, revealing an NDSB ligand bound to a novel site that is located in a fissure between the catalytic domain and the CAP module. The structure shows a half-open conformation of the CAP 1 module with a unique protruding loop of residues 150-155 that possesses a helical conformation in other structures of homologous PSPs. Activity assays indicate that the enzyme exhibits marginal PSP activity at low temperature but a sharp increase in the k(cat)/K(M) value, approximately 22 fold, when the temperature is increased. Structural and biochemical analyses suggest that the protruding loop in the active site might be an essential component for the regulation of the activity of PSP from hyperthermophilic T. onnurineus. Identification of this novel binding site distantly located from the catalytic site may be exploited for the development of effective therapeutic allosteric inhibitors against PSP activity. PubMed: 23239422DOI: 10.1002/PROT.24238 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.34 Å) |
Structure validation
Download full validation report
