3M71
Crystal Structure of Plant SLAC1 homolog TehA
Summary for 3M71
| Entry DOI | 10.2210/pdb3m71/pdb |
| Related | 3M72 3M74 3M75 3M76 3M77 3M78 3M7B 3M7C 3M7E 3M7L |
| Descriptor | Tellurite resistance protein tehA homolog, octyl beta-D-glucopyranoside (3 entities in total) |
| Functional Keywords | anion channel, alpha helical integral membrane protein, structural genomics, psi-2, protein structure initiative, new york consortium on membrane protein structure, nycomps, plant slac-1 homolog, unknown function |
| Biological source | Haemophilus influenzae |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : P44741 |
| Total number of polymer chains | 1 |
| Total formula weight | 36422.02 |
| Authors | Chen, Y.-H.,Hu, L.,Punta, M.,Bruni, R.,Hillerich, B.,Kloss, B.,Rost, B.,Love, J.,Siegelbaum, S.A.,Hendrickson, W.A.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2010-03-16, release date: 2010-05-12, Last modification date: 2024-02-21) |
| Primary citation | Chen, Y.H.,Hu, L.,Punta, M.,Bruni, R.,Hillerich, B.,Kloss, B.,Rost, B.,Love, J.,Siegelbaum, S.A.,Hendrickson, W.A. Homologue structure of the SLAC1 anion channel for closing stomata in leaves. Nature, 467:1074-1080, 2010 Cited by PubMed 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. PubMed: 20981093DOI: 10.1038/nature09487 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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