title: Crystal structure of phosphoramide-phosphorylated thymidylate synthase reveals pSer127, reflecting probably pHis to pSer phosphotransfer.
abstract: Crystal structure is presented of the binary complex between potassium phosphoramidate-phosphorylated recombinant C. elegans thymidylate synthase and dUMP. On each monomer a single phosphoserine residue (Ser127) was identified, instead of expected phosphohistidine. As (31)P NMR studies of both the phosphorylated protein and of potassium phosphoramidate potential to phosphorylate different amino acids point to histidine as the only possible site of the modification, thermodynamically favored intermolecular phosphotransfer from histidine to serine is suggested.
authors: Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland.
authors: Piotr
authors: P
authors: Wilk
authors: Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland.
authors: Adam
authors: A
authors: Jarmuła
authors: Rzeszów University of Technology, Faculty of Chemistry, Bioorganic Chemistry Laboratory, 6 Powstańców Warszawy Ave., 35-959 Rzeszów, Poland.
authors: Tomasz
authors: T
authors: Ruman
authors: Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland.
authors: Katarzyna
authors: K
authors: Banaszak
authors: Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland.
authors: Wojciech
authors: W
authors: Rypniewski
authors: Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland.
authors: Joanna
authors: J
authors: Cieśla
authors: Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland.
authors: Anna
authors: A
authors: Dowierciał
authors: Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland. Electronic address: rode@nencki.gov.pl.
authors: Wojciech
authors: W
authors: Rode
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000201:enzymology; D003460:Crystallization; D018360:Crystallography, X-Ray; D003856:Deoxyuracil Nucleotides / Q000737:chemistry; D006639:Histidine / Q000031:analogs & derivatives / Q000737:chemistry; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D063088:Phosphoramides / Q000737:chemistry*; D010766:Phosphorylation; D010768:Phosphoserine / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D013940:Thymidylate Synthase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D003856:Deoxyuracil Nucleotides; D063088:Phosphoramides; D011994:Recombinant Proteins; C005438:phosphoramide; D010768:Phosphoserine; D006639:Histidine; C007267:2'-deoxyuridylic acid; D013940:Thymidylate Synthase; C005436:phosphohistidine
keywords: Crystal structure; Phosphorylation; Phosphotransfer; Potassium phosphoramidate; Thymidylate synthase