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http://purl.uniprot.org/citations/31205021http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31205021http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31205021http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.org/dc/terms/identifier"doi:10.1107/s2059798319006867"xsd:string
http://purl.uniprot.org/citations/31205021http://purl.org/dc/terms/identifier"doi:10.1107/s2059798319006867"xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Wouters J."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Wouters J."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Leherte L."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Leherte L."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Haufroid M."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Haufroid M."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Mirgaux M."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/author"Mirgaux M."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/pages"592-604"xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/pages"592-604"xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/title"Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/title"Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase."xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/volume"75"xsd:string
http://purl.uniprot.org/citations/31205021http://purl.uniprot.org/core/volume"75"xsd:string
http://purl.uniprot.org/citations/31205021http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31205021
http://purl.uniprot.org/citations/31205021http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31205021