3NVA

Dimeric form of CTP synthase from Sulfolobus solfataricus

3NVA の概要

• エントリーDOI: 10.2210/pdb3nva/pdb
• 分子名称: CTP synthase (2 entities in total)
• 機能のキーワード: rossmann fold, ctp synthase activity, nucleotide binding, ligase
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 119667.34

構造登録者

Harris, P.,Willemoes, M.,Lauritsen, I.,Johansson, E.,Jensen, K.F. (登録日: 2010-07-08, 公開日: 2010-09-08, 最終更新日: 2023-11-01)

主引用文献

Lauritsen, I.,Willemoes, M.,Jensen, K.F.,Johansson, E.,Harris, P.
Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus
Acta Crystallogr.,Sect.F, 67:201-208, 2011

PubMed Abstract: CTP synthase catalyzes the last committed step in de novo pyrimidine-nucleotide biosynthesis. Active CTP synthase is a tetrameric enzyme composed of a dimer of dimers. The tetramer is favoured in the presence of the substrate nucleotides ATP and UTP; when saturated with nucleotide, the tetramer completely dominates the oligomeric state of the enzyme. Furthermore, phosphorylation has been shown to regulate the oligomeric states of the enzymes from yeast and human. The crystal structure of a dimeric form of CTP synthase from Sulfolobus solfataricus has been determined at 2.5 Å resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems. Residues that are involved in the tetramerization of S. solfataricus CTP synthase according to a structural alignment with the E. coli enzyme all have large thermal parameters in the dimeric form. Furthermore, they are seen to undergo substantial movement upon tetramerization.

PubMed: 21301086
DOI: 10.1107/S1744309110052334

実験手法

X-RAY DIFFRACTION (2.504 Å)