2W0N

Plasticity of PAS domain and potential role for signal transduction in the histidine-kinase DcuS

2W0N の概要

• エントリーDOI: 10.2210/pdb2w0n/pdb
• 関連するPDBエントリー: 1OJG
• 分子名称: SENSOR PROTEIN DCUS (1 entity in total)
• 機能のキーワード: signal transduction, two-component regulatory system, pas, dcus, kinase, membrane, transferase, solid state nmr, cell inner membrane, cell membrane, transmembrane, phosphoprotein
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0AEC8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13283.90

構造登録者

Etzkorn, M.,Kneuper, H.,Duennwald, P.,Vijayan, V.,Kraemer, J.,Griesinger, C.,Becker, S.,Unden, G.,Baldus, M. (登録日: 2008-08-19, 公開日: 2008-09-30, 最終更新日: 2024-05-15)

主引用文献

Etzkorn, M.,Kneuper, H.,Duennwald, P.,Vijayan, V.,Kraemer, J.,Griesinger, C.,Becker, S.,Unden, G.,Baldus, M.
Plasticity of the Pas Domain and a Potential Role for Signal Transduction in the Histidine Kinase Dcus.
Nat.Struct.Mol.Biol., 15:1031-, 2008

PubMed Abstract: The mechanistic understanding of how membrane-embedded sensor kinases recognize signals and regulate kinase activity is currently limited. Here we report structure-function relationships of the multidomain membrane sensor kinase DcuS using solid-state NMR, structural modeling and mutagenesis. Experimental data of an individual cytoplasmic Per-Arnt-Sim (PAS) domain were compared to structural models generated in silico. These studies, together with previous NMR work on the periplasmic PAS domain, enabled structural investigations of a membrane-embedded 40-kDa construct by solid-state NMR, comprising both PAS segments and the membrane domain. Structural alterations are largely limited to protein regions close to the transmembrane segment. Data from isolated and multidomain constructs favor a disordered N-terminal helix in the cytoplasmic domain. Mutations of residues in this region strongly influence function, suggesting that protein flexibility is related to signal transduction toward the kinase domain and regulation of kinase activity.

PubMed: 18820688
DOI: 10.1038/NSMB.1493

実験手法

SOLID-STATE NMR