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Seeing How Ion Channels Work - Structural Analysis of SLAC1-family Anion Channel Activity

日期: 2011-11-03
学术报告
Seeing How Ion Channels Work
- Structural Analysis of SLAC1-family Anion Channel Activity
报告人: Yu-Hang Chen, Ph.D.
Department of Biochemistry and Molecular Biophysics,
Columbia University, New York.
时间: 13:30, November 3.
地点: 生命科学学院411会议室.
The plant SLAC1 anion channel controls turgor pressure in the aperture- defining guard cells of plant stomata, thereby regulating the exchange of water vapour and photosynthetic gases in response to environmental signals such as droughtor high CO2. Here we determine the crystal structure of a bacterial homologue (Haemophilus influenzae) of SLAC1 at 1.20 ? resolution, and use structure-inspired mutagenesis to analyze the conductance properties of SLAC1 channels. SLAC1 is a symmetrical trimer composed from quasi-symmetrical subunits, each having ten transmembrane helices arranged from helical hairpin pairs to form a central five-helix transmembrane pore that is gated by an extremely conserved phenylalanine residue. Conformational features indicate a mechanismfor control of gating by kinase activation, and electrostatic features of the pore coupled with electrophysiological characteristics indicate that selectivity among different anions is largely a function of the energetic cost of ion dehydration.
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