6q6j

Human phosphoserine phosphatase with substrate analogue homo-cysteic acid

spinqualitylabelsall models 6q6j, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6q6j is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.985Å Ligands: CA, CL, HJT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease SERB_HUMAN Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:614023. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome. Function SERB_HUMAN Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Publication Abstract from PubMed 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 A) 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. Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase.,Haufroid M, Mirgaux M, Leherte L, Wouters J Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):592-604. doi:, 10.1107/S2059798319006867. Epub 2019 Jun 4. PMID:31205021 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoserine phosphatase

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