Structural highlights
Publication Abstract from PubMed
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 31P 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.
Crystal structure of phosphoramide-phosphorylated thymidylate synthase reveals pSer127, reflecting probably pHis to pSer phosphotransfer.,Wilk P, Jarmula A, Ruman T, Banaszak K, Rypniewski W, Ciesla J, Dowiercial A, Rode W Bioorg Chem. 2013 Nov 21;52C:44-49. doi: 10.1016/j.bioorg.2013.11.003. PMID:24321279[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wilk P, Jarmula A, Ruman T, Banaszak K, Rypniewski W, Ciesla J, Dowiercial A, Rode W. Crystal structure of phosphoramide-phosphorylated thymidylate synthase reveals pSer127, reflecting probably pHis to pSer phosphotransfer. Bioorg Chem. 2013 Nov 21;52C:44-49. doi: 10.1016/j.bioorg.2013.11.003. PMID:24321279 doi:http://dx.doi.org/10.1016/j.bioorg.2013.11.003
