4ISW

Crystal Structure of Phosphorylated C.elegans Thymidylate Synthase in Complex with dUMP

Summary for 4ISW

• Entry DOI: 10.2210/pdb4isw/pdb
• Related: 3IHI 4E5O 4G9U 4IQB 4IQQ 4IRR
• Descriptor: Thymidylate synthase, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: phosphoprotein, protein homodimer, deoxynucleotide biosynthesis, phosphorylation, transferase
• Biological source: Caenorhabditis elegans (nematode)
• Total number of polymer chains: 2
• Total formula weight: 72488.13

Authors

Wilk, P.,Dowiercial, A.,Banaszak, K.,Jarmula, A.,Rypniewski, W.,Rode, W. (deposition date: 2013-01-17, release date: 2013-12-11, Last modification date: 2024-11-06)

Primary citation

Wilk, P.,Jarmua, A.,Ruman, T.,Banaszak, K.,Rypniewski, W.,Ciesla, J.,Dowiercia, A.,Rode, W.
Crystal structure of phosphoramide-phosphorylated thymidylate synthase reveals pSer127, reflecting probably pHis to pSer phosphotransfer.
Bioorg.Chem., 52C:44-49, 2013

PubMed 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.

PubMed: 24321279
DOI: 10.1016/j.bioorg.2013.11.003

Experimental method

X-RAY DIFFRACTION (3.14 Å)