6HYJ
PSPH Human phosphoserine phosphatase
Summary for 6HYJ
| Entry DOI | 10.2210/pdb6hyj/pdb |
| Descriptor | Phosphoserine phosphatase, PHOSPHOSERINE, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | phosphoserine phosphatase, homo sapiens, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 50402.56 |
| Authors | Wouters, J.,Haufroid, M.,Mirgaux, M. (deposition date: 2018-10-22, release date: 2019-06-12, Last modification date: 2024-01-31) |
| Primary citation | Haufroid, M.,Mirgaux, M.,Leherte, L.,Wouters, J. Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase. Acta Crystallogr D Struct Biol, 75:592-604, 2019 Cited by PubMed Abstract: The equilibrium between phosphorylation and dephosphorylation is one of the most important processes that takes place in living cells. Human phosphoserine phosphatase (hPSP) is a key enzyme in the production of serine by the dephosphorylation of phospho-L-serine. It is directly involved in the biosynthesis of other important metabolites such as glycine and D-serine (a neuromodulator). hPSP is involved in the survival mechanism of cancer cells and has recently been found to be an essential biomarker. Here, three new high-resolution crystal structures of hPSP (1.5-2.0 Å) in complexes with phosphoserine and with serine, which are the substrate and the product of the reaction, respectively, and in complex with a noncleavable substrate analogue (homocysteic acid) are presented. New types of interactions take place between the enzyme and its ligands. Moreover, the loop involved in the open/closed state of the enzyme is fully refined in a totally unfolded conformation. This loop is further studied through molecular-dynamics simulations. Finally, all of these analyses allow a more complete reaction mechanism for this enzyme to be proposed which is consistent with previous publications on the subject. PubMed: 31205021DOI: 10.1107/S2059798319006867 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.929 Å) |
Structure validation
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