期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 108, 期 51, 页码 20802-20807出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1111149108
关键词
conformational changes; cyclic nucleotide gating; membrane protein; MloK1; single-molecule imaging
资金
- Deutsche Forschungsgemeinschaft
- European Union
- European Life Scientist Organization
- Klaus Tschira Stiftung
- Swiss National Science Foundation
- Fundacao para a Ciencia e a Tecnologia [SFRH/BD/60274/2009]
- European Molecular Biology Organization
- Fundação para a Ciência e a Tecnologia [SFRH/BD/60274/2009] Funding Source: FCT
Cyclic nucleotide-regulated ion channels are present in bacteria, plants, vertebrates, and humans. In higher organisms, they are closely involved in signaling networks of vision and olfaction. Binding of cAMPor cGMP favors the activation of these ion channels. Despite a wealth of structural and studies, there is a lack of structural data describing the gating process in a full-length cyclic nucleotide-regulated channel. We used high-resolution atomic force microscopy (AFM) to directly observe the conformational change of the membrane embedded bacterial cyclic nucleotide-regulated channel MlotiK1. In the nucleotide-bound conformation, the cytoplasmic cyclic nucleotide-binding (CNB) domains of MlotiK1 are disposed in a fourfold symmetric arrangement forming a pore-like vestibule. Upon nucleotide-unbinding, the four CNB domains undergo a large rearrangement, stand up by similar to 1.7 nm, and adopt a structurally variable grouped conformation that closes the cytoplasmic vestibule. This fully reversible conformational change provides insight into how CNB domains rearrange when regulating the potassium channel.
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