Crystal structure of phosphoramide-phosphorylated thymidylate synthase reveals pSer127, reflecting probably pHis to pSer phosphotransfer.
Bioorg Chem
; 52: 44-9, 2014 Feb.
Article
in En
| MEDLINE
| ID: mdl-24321279
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phosphoserine
/
Thymidylate Synthase
/
Phosphoramides
Limits:
Animals
Language:
En
Journal:
Bioorg Chem
Year:
2014
Type:
Article
Affiliation country:
Poland