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, Wayne A. Hendrickson

Research output: Contribution to journalArticlepeer-review

81 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1074-1080
Number of pages7
JournalNature
Volume467
Issue number7319
DOIs
StatePublished - Oct 28 2010

ASJC Scopus subject areas

  • General

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