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

TitleHomologue structure of the SLAC1 anion channel for closing stomata in leaves.
Publication TypeJournal Article
Year of Publication2010
AuthorsChen, Y-H, Hu, L, Punta, M, Bruni, R, Hillerich, B, Kloss, B, Rost, B, Love, J, Siegelbaum, SA, Hendrickson, WA
Date Published2010 Oct 28
KeywordsAmino Acid Sequence, Animals, Arabidopsis, Arabidopsis Proteins, Bacterial Proteins, Crystallography, X-Ray, Electric Conductivity, Haemophilus influenzae, Ion Channel Gating, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Oocytes, Phenylalanine, Plant Stomata, Static Electricity, Structural Homology, Protein, Substrate Specificity, Xenopus laevis

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.

Alternate JournalNature
PubMed ID20981093
PubMed Central IDPMC3548404
Grant ListR01 GM034102 / GM / NIGMS NIH HHS / United States
U54 GM075026 / GM / NIGMS NIH HHS / United States
U54 GM095315 / GM / NIGMS NIH HHS / United States