3fd5

Crystal structure of human selenophosphate synthetase 1 complex with AMPCP

spinqualitylabelsall models 3fd5, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fd5 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. Ligands: AP2, K, MG, PO4 Related: 2yye, 3fd6 Gene: SEPHS1, SELD, SPS, SPS1 (Homo sapiens) Activity: Selenide, water dikinase, with EC number 2.7.9.3 Resources: FirstGlance, OCA, RCSB, PDBsum Function [SPS1_HUMAN] Synthesizes selenophosphate from selenide and ATP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Selenophosphate synthetase catalyzes the synthesis of the highly active selenium donor molecule selenophosphate, a key intermediate in selenium metabolism. We have determined the high-resolution crystal structure of human selenophosphate synthetase 1 (hSPS1). An unexpected reaction intermediate, with a tightly bound phosphate and ADP at the active site has been captured in the structure. An enzymatic assay revealed that hSPS1 possesses low ADP hydrolysis activity in the presence of phosphate. Our structural and enzymatic results suggest that consuming the second high-energy phosphoester bond of ATP could protect the labile product selenophosphate during catalytic reaction. We solved another hSPS1 structure with potassium ions at the active sites. Comparing the two structures, we were able to define the monovalent cation-binding site of the enzyme. The detailed mechanism of the ADP hydrolysis step and the exact function of the monovalent cation for hSPS1 catalytic reaction are proposed. Crystal structures of catalytic intermediates of human selenophosphate synthetase 1.,Wang KT, Wang J, Li LF, Su XD J Mol Biol. 2009 Jul 24;390(4):747-59. Epub 2009 May 25. PMID:19477186 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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