Phosphoserine phosphatase

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spinqualitylabelsall models Human phosphoserine phosphatase dimer complex with serine and phosphate 1l8o Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Phosphoserine phosphatase (PSP) catalyzes the dephosphorylation of phosphoserine to produce serine and phosphate. This is the last reaction in serine biosynthesis. PSP is part of the glycine, serine and threonine metabolism[1]. Mg+2 ion is a cofactor of PSP. Disease Mutations of PSP were found in patients with Williams syndrome[2]. Structural highlights The human PSP overall structure contains a large core domain and a smaller 4-helix bundle domain. The active site is located in a cleft between the 2 domains[3].

3D structures of phosphoserine phosphatase

Updated on 29-August-2016

References

1. ↑ NEUHAUS FC, BYRNE WL. Metabolism of phosphoserine. II. Purification and properties of O-phosphoserine phosphatase. J Biol Chem. 1959 Jan;234(1):113-21. PMID:13610904
2. ↑ Jaeken J, Detheux M, Fryns JP, Collet JF, Alliet P, Van Schaftingen E. Phosphoserine phosphatase deficiency in a patient with Williams syndrome. J Med Genet. 1997 Jul;34(7):594-6. PMID:9222972
3. ↑ Kim HY, Heo YS, Kim JH, Park MH, Moon J, Kim E, Kwon D, Yoon J, Shin D, Jeong EJ, Park SY, Lee TG, Jeon YH, Ro S, Cho JM, Hwang KY. Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase. J Biol Chem. 2002 Nov 29;277(48):46651-8. Epub 2002 Sep 3. PMID:12213811 doi:10.1074/jbc.M204866200