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3.1.3.3: phosphoserine phosphatase

This is an abbreviated version!
For detailed information about phosphoserine phosphatase, go to the full flat file.

Word Map on EC 3.1.3.3

Reaction

O-phospho-L(or D)-serine
+
H2O
=
L(or D)-serine
 +
phosphate

Synonyms

3-phosphoserine phosphatase, BSU04700, BSU04740, BSU34110, CTD phosphatase fcp1, HPSP, iPSP, iPSP1, iPSP2, L-phosphoserine phosphatase, metal-independent phosphoserine phosphatase, metal-independent PSP, More, O-phosphoserine phosphohydrolase, phosphatase, phosphoserine, phosphoserine phosphatase, phosphoserine phosphatase RsbP, phosphoserine phosphatase RsbU, phosphoserine phosphatase RsbX, phosphoserine:homoserine phosphotransferase, PP1, PSP, PSP1, pspA, PSPase, pspB, PSPH, RsbP, RsbU, RsbX, SerB, SerB PG0653, SerB2, SerB653, serine/threonine protein phosphatase, sigma-B negative effector, StP, THrH, TON_1161, yvfP

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.3 phosphoserine phosphatase

Crystallization

Crystallization on EC 3.1.3.3 - phosphoserine phosphatase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour-diffusion method. A resolution of 1.53 A provides a detailed model of the active site in a completely open conformation and the water molecules bound to it
-
hanging-drop vapour diffusion method
-
hanging-drop vapour-diffusion method
-
replacement of sixfold coordinated Mg2+ in active site by Ca2+ results in sevenfold coordinated metal ion, explaining the inhibitory effect of Ca2+
-
apo-form and in complex with its substrate L-phosphoserine, to 1.5 A and 1.8 A resolution, respectively. In the crystal structure of the enzyme-substrate complex, oxygen atoms of the carboxyl group of L-phosphoserine form hydrogen bonds with main-chain amides of Gln21 and Gly22, and Nepsilon2 of Gln21, and partly form a hydrogen or an ionic bond withNepsilon2 of His85. The nitrogen atom of amino group of L-phosphoserine forms a hydrogen or an ionic bond with oxygen atoms of the side-chain carboxyl group of Glu82, and forms hydrogen bonds with Nepsilon2 of His85 and Ogamma1 of Thr15
two diffraction data sets with resolution ranges of 45.0-2.50 and 45.0-1.50 A. The space group of the crystal is orthorhombic P212121, with unit-cell parameters a = 49.8, b = 73.6, c = 124.3 A
crystals are grown by using the hanging drop vapor diffusion method with seeding.1.5 A resolution the X-ray crystal structure of the complex of BeF3 2 with phosphoserine phosphatase. The structure is comparable to that of a phosphoenzyme intermediate: BeF3- is bound to Asp11 with the tetrahedral geometry of a phosphoryl group, is coordinated to Mg2+, and is bound to residues surrounding the active site that are conserved in the haloacid dehalogenase (HAD) superfamily
hanging-drop vapor-diffusion method, crystal structure determined at 1.8 A resolution
-
high-resolution, 1.5-1.9 A structures which define the open state prior to substrate binding, the complex with phosphoserine substrate bound, and the complex with AlF3, a transition-state analog for the phospho-transfer steps in the reaction
construction of a homology model and molecular docking of O-phospho-L-serine. Residues Asp185, Ser273, Lys-318, and Asp-341 are part of the substrate binding pocket. Val186 and Ser188 might also interact with O-phospho-L-serine
hanging-drop vapour diffsuion method
-
sitting drop method at 18 °C, crystal structure of the enzyme at 1.8 A resolution