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Title | Homologue structure of the SLAC1 anion channel for closing stomata in leaves. |
Publication Type | Journal Article |
Year of Publication | 2010 |
Authors | Chen, Y-H, Hu, L, Punta, M, Bruni, R, Hillerich, B, Kloss, B, Rost, B, Love, J, Siegelbaum, SA, Hendrickson, WA |
Journal | Nature |
Volume | 467 |
Issue | 7319 |
Pagination | 1074-80 |
Date Published | 2010 Oct 28 |
ISSN | 1476-4687 |
Keywords | Amino 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 |
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. |
DOI | 10.1038/nature09487 |
Alternate Journal | Nature |
PubMed ID | 20981093 |
PubMed Central ID | PMC3548404 |
Grant List | R01 GM034102 / GM / NIGMS NIH HHS / United States U54 GM075026 / GM / NIGMS NIH HHS / United States U54 GM095315 / GM / NIGMS NIH HHS / United States |