1DC7

STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL TRANSDUCTION

1DC7 の概要

• エントリーDOI: 10.2210/pdb1dc7/pdb
• 関連するPDBエントリー: 1DC8 1NTR
• NMR情報: BMRB: 4527
• 分子名称: NITROGEN REGULATION PROTEIN (1 entity in total)
• 機能のキーワード: receiver domain, phosphorylation, signal transduction, conformational rearrangement, two-component system, signaling protein
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13636.60

構造登録者

Kern, D.,Volkman, B.F.,Luginbuhl, P.,Nohaile, M.J.,Kustu, S.,Wemmer, D.E. (登録日: 1999-11-04, 公開日: 2000-01-05, 最終更新日: 2024-05-22)

主引用文献

Kern, D.,Volkman, B.F.,Luginbuhl, P.,Nohaile, M.J.,Kustu, S.,Wemmer, D.E.
Structure of a transiently phosphorylated switch in bacterial signal transduction.
Nature, 402:894-898, 1999

PubMed Abstract: Receiver domains are the dominant molecular switches in bacterial signalling. Although several structures of non-phosphorylated receiver domains have been reported, a detailed structural understanding of the activation arising from phosphorylation has been impeded by the very short half-lives of the aspartylphosphate linkages. Here we present the first structure of a receiver domain in its active state, the phosphorylated receiver domain of the bacterial enhancer-binding protein NtrC (nitrogen regulatory protein C). Nuclear magnetic resonance spectra were taken during steady-state autophosphorylation/dephosphorylation, and three-dimensional spectra from multiple samples were combined. Phosphorylation induces a large conformational change involving a displacement of beta-strands 4 and 5 and alpha-helices 3 and 4 away from the active site, a register shift and an axial rotation in helix 4. This creates an exposed hydrophobic surface that is likely to transmit the signal to the transcriptional activation domain.

PubMed: 10622255
DOI: 10.1038/47273

実験手法

SOLUTION NMR