1VCM

Crystal Structure of T.th. HB8 CTP synthetase

1VCM の概要

• エントリーDOI: 10.2210/pdb1vcm/pdb
• 関連するPDBエントリー: 1VCN 1VCO
• 分子名称: CTP synthetase (2 entities in total)
• 機能のキーワード: tetramer, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61086.91

構造登録者

Goto, M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-03-10, 公開日: 2004-08-31, 最終更新日: 2023-12-27)

主引用文献

Goto, M.,Omi, R.,Nakagawa, N.,Miyahara, I.,Hirotsu, K.
Crystal Structures of CTP Synthetase Reveal ATP, UTP, and Glutamine Binding Sites
Structure, 12:1413-1423, 2004

PubMed Abstract: CTP synthetase (CTPs) catalyzes the last step in CTP biosynthesis, in which ammonia generated at the glutaminase domain reacts with the ATP-phosphorylated UTP at the synthetase domain to give CTP. Glutamine hydrolysis is active in the presence of ATP and UTP and is stimulated by the addition of GTP. We report the crystal structures of Thermus thermophilus HB8 CTPs alone, CTPs with 3SO4(2-), and CTPs with glutamine. The enzyme is folded into a homotetramer with a cross-shaped structure. Based on the binding mode of sulfate anions to the synthetase site, ATP and UTP are computer modeled into CTPs with a geometry favorable for the reaction. Glutamine bound to the glutaminase domain is situated next to the triad of Glu-His-Cys as a catalyst and a water molecule. Structural information provides an insight into the conformational changes associated with the binding of ATP and UTP and the formation of the GTP binding site.

PubMed: 15296735
DOI: 10.1016/j.str.2004.05.013

実験手法

X-RAY DIFFRACTION (2.35 Å)