4ISW

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

4ISW の概要

• エントリーDOI: 10.2210/pdb4isw/pdb
• 関連するPDBエントリー: 3IHI 4E5O 4G9U 4IQB 4IQQ 4IRR
• 分子名称: Thymidylate synthase, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: phosphoprotein, protein homodimer, deoxynucleotide biosynthesis, phosphorylation, transferase
• 由来する生物種: Caenorhabditis elegans (nematode)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72488.13

構造登録者

Wilk, P.,Dowiercial, A.,Banaszak, K.,Jarmula, A.,Rypniewski, W.,Rode, W. (登録日: 2013-01-17, 公開日: 2013-12-11, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.14 Å)