7fhl

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Structure of AtTPC1 with 50 mM Ca2+

Structural highlights

7fhl is a 4 chain structure with sequence from Arabidopsis thaliana and Human orthopneumovirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.1Å
Ligands:CA
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPC1_ARATH Functions as a voltage-gated inward-rectifying Ca(2+) channel (VDCC) across the vacuole membrane. Is one of the essential components of the slow vacuolar (SV) channel. Acts as the major ROS-responsive Ca(2+) channel and is the possible target of Al-dependent inhibition. Involved in the regulation of germination and stomatal movement.[1] [2] GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.

Publication Abstract from PubMed

Arabidopsis thaliana two-pore channel AtTPC1 is a voltage-gated, Ca(2+)-modulated, nonselective cation channel that is localized in the vacuolar membrane and responsible for generating slow vacuolar (SV) current. Under depolarizing membrane potential, cytosolic Ca(2+) activates AtTPC1 by binding at the EF-hand domain, whereas luminal Ca(2+) inhibits the channel by stabilizing the voltage-sensing domain II (VSDII) in the resting state. Here, we present 2.8 to 3.3 A cryoelectron microscopy (cryo-EM) structures of AtTPC1 in two conformations, one in closed conformation with unbound EF-hand domain and resting VSDII and the other in a partially open conformation with Ca(2+)-bound EF-hand domain and activated VSDII. Structural comparison between the two different conformations allows us to elucidate the structural mechanisms of voltage gating, cytosolic Ca(2+) activation, and their coupling in AtTPC1. This study also provides structural insight into the general voltage-gating mechanism among voltage-gated ion channels.

Voltage-gating and cytosolic Ca(2+) activation mechanisms of Arabidopsis two-pore channel AtTPC1.,Ye F, Xu L, Li X, Zeng W, Gan N, Zhao C, Yang W, Jiang Y, Guo J Proc Natl Acad Sci U S A. 2021 Dec 7;118(49). pii: 2113946118. doi:, 10.1073/pnas.2113946118. PMID:34845029[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
6 reviews cite this structure
Calcium channels and transporters: Roles in response to biotic and abiotic stresses.
Park et al. (2022)
5 more
5 other articles
No citations found

See Also

References

  1. ↑ Kawano T, Kadono T, Fumoto K, Lapeyrie F, Kuse M, Isobe M, Furuichi T, Muto S. Aluminum as a specific inhibitor of plant TPC1 Ca2+ channels. Biochem Biophys Res Commun. 2004 Nov 5;324(1):40-5. PMID:15464979 doi:http://dx.doi.org/S0006-291X(04)02051-0
  2. ↑ Peiter E, Maathuis FJ, Mills LN, Knight H, Pelloux J, Hetherington AM, Sanders D. The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement. Nature. 2005 Mar 17;434(7031):404-8. PMID:15772667 doi:http://dx.doi.org/nature03381
  3. ↑ Ye F, Xu L, Li X, Zeng W, Gan N, Zhao C, Yang W, Jiang Y, Guo J. Voltage-gating and cytosolic Ca(2+) activation mechanisms of Arabidopsis two-pore channel AtTPC1. Proc Natl Acad Sci U S A. 2021 Dec 7;118(49). pii: 2113946118. doi:, 10.1073/pnas.2113946118. PMID:34845029 doi:http://dx.doi.org/10.1073/pnas.2113946118

Contents


PDB ID 7fhl

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OCA

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