5E1J
Structure of voltage-gated two-pore channel TPC1 from Arabidopsis thaliana
Summary for 5E1J
| Entry DOI | 10.2210/pdb5e1j/pdb |
| Descriptor | Two pore calcium channel protein 1, BARIUM ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | two-pore channel, voltage-gated, calcium modulation, metal transport |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 86902.51 |
| Authors | |
| Primary citation | Guo, J.,Zeng, W.,Chen, Q.,Lee, C.,Chen, L.,Yang, Y.,Cang, C.,Ren, D.,Jiang, Y. Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana. Nature, 531:196-201, 2016 Cited by PubMed Abstract: Two-pore channels (TPCs) contain two copies of a Shaker-like six-transmembrane (6-TM) domain in each subunit and are ubiquitously expressed in both animals and plants as organellar cation channels. Here we present the crystal structure of a vacuolar two-pore channel from Arabidopsis thaliana, AtTPC1, which functions as a homodimer. AtTPC1 activation requires both voltage and cytosolic Ca(2+). Ca(2+) binding to the cytosolic EF-hand domain triggers conformational changes coupled to the pair of pore-lining inner helices from the first 6-TM domains, whereas membrane potential only activates the second voltage-sensing domain, the conformational changes of which are coupled to the pair of inner helices from the second 6-TM domains. Luminal Ca(2+) or Ba(2+) can modulate voltage activation by stabilizing the second voltage-sensing domain in the resting state and shift voltage activation towards more positive potentials. Our Ba(2+)-bound AtTPC1 structure reveals a voltage sensor in the resting state, providing hitherto unseen structural insight into the general voltage-gating mechanism among voltage-gated channels. PubMed: 26689363DOI: 10.1038/nature16446 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.308 Å) |
Structure validation
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