2Y3B

Co-bound form of Cupriavidus metallidurans CH34 CnrXs

2Y3B の概要

• エントリーDOI: 10.2210/pdb2y3b/pdb
• 関連するPDBエントリー: 2Y39 2Y3D 2Y3G 2Y3H
• 分子名称: NICKEL AND COBALT RESISTANCE PROTEIN CNRR, COBALT (II) ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: metal binding protein
• 由来する生物種: CUPRIAVIDUS METALLIDURANS
• 細胞内の位置: Periplasm: P37975
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13647.09

構造登録者

Trepreau, J.,Girard, E.,Maillard, A.P.,de Rosny, E.,Petit-Haertlein, I.,Kahn, R.,Coves, J. (登録日: 2010-12-20, 公開日: 2011-03-30, 最終更新日: 2024-05-08)

主引用文献

Trepreau, J.,Girard, E.,Maillard, A.P.,De Rosny, E.,Petit-Haertlein, I.,Kahn, R.,Coves, J.
Structural Basis for Metal Sensing by Cnrx.
J.Mol.Biol., 408:766-, 2011

PubMed Abstract: CnrX is the metal sensor and signal modulator of the three-protein transmembrane signal transduction complex CnrYXH of Cupriavidus metallidurans CH34 that is involved in the setup of cobalt and nickel resistance. We have determined the atomic structure of the soluble domain of CnrX in its Ni-bound, Co-bound, or Zn-bound form. Ni and Co ions elicit a biological response, while the Zn-bound form is inactive. The structures presented here reveal the topology of intraprotomer and interprotomer interactions and the ability of metal-binding sites to fine-tune the packing of CnrX dimer as a function of the bound metal. These data suggest an allosteric mechanism to explain how the complex is switched on and how the signal is modulated by Ni or Co binding. These results provide clues to propose a model for signal propagation through the membrane in the complex.

PubMed: 21414325
DOI: 10.1016/J.JMB.2011.03.014

実験手法

X-RAY DIFFRACTION (1.554 Å)