3GIG

Crystal structure of phosphorylated DesKC in complex with AMP-PCP

3GIG の概要

• エントリーDOI: 10.2210/pdb3gig/pdb
• 関連するPDBエントリー: 3EHF 3GIE 3GIF
• 分子名称: Sensor histidine kinase desK, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: four-helix bundle, ghl atpase domain, cell membrane, kinase, membrane, phosphoprotein, transferase, transmembrane, two-component regulatory system
• 由来する生物種: Bacillus subtilis; 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Potential): O34757 O34757
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51069.24

構造登録者

Trajtenberg, F.,Albanesi, D.,Alzari, P.M.,Buschiazzo, A.,de Mendoza, D. (登録日: 2009-03-05, 公開日: 2009-09-15, 最終更新日: 2023-11-01)

主引用文献

Albanesi, D.,Martin, M.,Trajtenberg, F.,Mansilla, M.C.,Haouz, A.,Alzari, P.M.,de Mendoza, D.,Buschiazzo, A.
Structural plasticity and catalysis regulation of a thermosensor histidine kinase
Proc.Natl.Acad.Sci.USA, 106:16185-16190, 2009

PubMed Abstract: Temperature sensing is essential for the survival of living cells. A major challenge is to understand how a biological thermometer processes thermal information to optimize cellular functions. Using structural and biochemical approaches, we show that the thermosensitive histidine kinase, DesK, from Bacillus subtilis is cold-activated through specific interhelical rearrangements in its central four-helix bundle domain. As revealed by the crystal structures of DesK in different functional states, the plasticity of this helical domain influences the catalytic activities of the protein, either by modifying the mobility of the ATP-binding domains for autokinase activity or by modulating binding of the cognate response regulator to sustain the phosphotransferase and phosphatase activities. The structural and biochemical data suggest a model in which the transmembrane sensor domain of DesK promotes these structural changes through conformational signals transmitted by the membrane-connecting two-helical coiled-coil, ultimately controlling the alternation between output autokinase and phosphatase activities. The structural comparison of the different DesK variants indicates that incoming signals can take the form of helix rotations and asymmetric helical bends similar to those reported for other sensing systems, suggesting that a similar switching mechanism could be operational in a wide range of sensor histidine kinases.

PubMed: 19805278
DOI: 10.1073/pnas.0906699106

実験手法

X-RAY DIFFRACTION (3.502 Å)