7EN0
Structure and Activity of SLAC1 Channels for Stomatal Signaling in Leaves
Summary for 7EN0
| Entry DOI | 10.2210/pdb7en0/pdb |
| EMDB information | 31197 |
| Descriptor | SLow Anion Channel 1, DIUNDECYL PHOSPHATIDYL CHOLINE, SPHINGOSINE (3 entities in total) |
| Functional Keywords | anion channel, membrane protein |
| Biological source | Brachypodium distachyon (Purple false brome, Trachynia distachya) |
| Total number of polymer chains | 3 |
| Total formula weight | 190802.02 |
| Authors | |
| Primary citation | Deng, Y.N.,Kashtoh, H.,Wang, Q.,Zhen, G.X.,Li, Q.Y.,Tang, L.H.,Gao, H.L.,Zhang, C.R.,Qin, L.,Su, M.,Li, F.,Huang, X.H.,Wang, Y.C.,Xie, Q.,Clarke, O.B.,Hendrickson, W.A.,Chen, Y.H. Structure and activity of SLAC1 channels for stomatal signaling in leaves. Proc.Natl.Acad.Sci.USA, 118:-, 2021 Cited by PubMed Abstract: Stomata in leaves regulate gas exchange between the plant and its atmosphere. Various environmental stimuli elicit abscisic acid (ABA); ABA leads to phosphoactivation of slow anion channel 1 (SLAC1); SLAC1 activity reduces turgor pressure in aperture-defining guard cells; and stomatal closure ensues. We used electrophysiology for functional characterizations of SLAC1 (SLAC1) and cryoelectron microscopy (cryo-EM) for structural analysis of SLAC1 (SLAC1), at 2.97-Å resolution. We identified 14 phosphorylation sites in SLAC1 and showed nearly 330-fold channel-activity enhancement with 4 to 6 of these phosphorylated. Seven SLAC1-conserved arginines are poised in SLAC1 for regulatory interaction with the N-terminal extension. This SLAC1 structure has its pores closed, in a basal state, spring loaded by phenylalanyl residues in high-energy conformations. SLAC1 phosphorylation fine-tunes an equilibrium between basal and activated SLAC1 trimers, thereby controlling the degree of stomatal opening. PubMed: 33926963DOI: 10.1073/pnas.2015151118 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.97 Å) |
Structure validation
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