Homologue structure of the SLAC1 anion channel for closing stomata in leaves

Yu-hang Chen, Lei Hu, Marco Punta, Renato Bruni, Brandan Hillerich, Brian Kloss, Burkhard Rost, James Love, Steven A. Siegelbaum and Wayne A. Hendrickson ()
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Yu-hang Chen: Columbia University
Lei Hu: Columbia University
Marco Punta: NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
Renato Bruni: NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
Brandan Hillerich: NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
Brian Kloss: NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
Burkhard Rost: Columbia University
James Love: NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
Steven A. Siegelbaum: Columbia University
Wayne A. Hendrickson: Columbia University

Nature, 2010, vol. 467, issue 7319, 1074-1080

Abstract: Abstract 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 drought or high levels of carbon dioxide. Here we determine the crystal structure of a bacterial homologue (Haemophilus influenzae) of SLAC1 at 1.20 Å resolution, and use structure-inspired mutagenesis to analyse 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 mechanism for 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.

Date: 2010
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DOI: 10.1038/nature09487

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