2FTK

berylloflouride Spo0F complex with Spo0B

2FTK の概要

• エントリーDOI: 10.2210/pdb2ftk/pdb
• 関連するPDBエントリー: 1F51 1IXM 1SRR
• 分子名称: Sporulation initiation phosphotransferase B, Sporulation initiation phosphotransferase F, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: sporulation, spo0f, spo0b phosphorelay, transferase
• 由来する生物種: Bacillus subtilis; 詳細
• 細胞内の位置: Cytoplasm: P06535; Cytoplasm (Probable): P06628
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 147325.71

構造登録者

Varughese, K.I. (登録日: 2006-01-24, 公開日: 2006-07-18, 最終更新日: 2024-11-20)

主引用文献

Varughese, K.I.,Tsigelny, I.,Zhao, H.
The Crystal Structure of Beryllofluoride Spo0F in Complex with the Phosphotransferase Spo0B Represents a Phosphotransfer Pretransition State.
J.Bacteriol., 188:4970-4977, 2006

PubMed Abstract: A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.

PubMed: 16788205
DOI: 10.1128/JB.00160-06

実験手法

X-RAY DIFFRACTION (3.05 Å)