7YVC

Aplysia californica FaNaC in apo state

Summary for 7YVC

• Entry DOI: 10.2210/pdb7yvc/pdb
• EMDB information: 34123
• Descriptor: FMRFamide-gated Na+ channel, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: neuropeptide, ion channel, fmrfamide, transport protein
• Biological source: Aplysia californica (California sea hare); More
• Total number of polymer chains: 3
• Total formula weight: 236375.07

Authors

Chen, Q.F.,Liu, F.L.,Dang, Y.,Feng, H.,Zhang, Z.,Ye, S. (deposition date: 2022-08-19, release date: 2023-08-09, Last modification date: 2024-11-13)

Primary citation

Liu, F.,Dang, Y.,Li, L.,Feng, H.,Li, J.,Wang, H.,Zhang, X.,Zhang, Z.,Ye, S.,Tian, Y.,Chen, Q.
Structure and mechanism of a neuropeptide-activated channel in the ENaC/DEG superfamily.
Nat.Chem.Biol., 19:1276-1285, 2023

PubMed Abstract: Phe-Met-Arg-Phe-amide (FMRFamide)-activated sodium channels (FaNaCs) are a family of channels activated by the neuropeptide FMRFamide, and, to date, the underlying ligand gating mechanism remains unknown. Here we present the high-resolution cryo-electron microscopy structures of Aplysia californica FaNaC in both apo and FMRFamide-bound states. AcFaNaC forms a chalice-shaped trimer and possesses several notable features, including two FaNaC-specific insertion regions, a distinct finger domain and non-domain-swapped transmembrane helix 2 in the transmembrane domain (TMD). One FMRFamide binds to each subunit in a cleft located in the top-most region of the extracellular domain, with participation of residues from the neighboring subunit. Bound FMRFamide adopts an extended conformation. FMRFamide binds tightly to A. californica FaNaC in an N terminus-in manner, which causes collapse of the binding cleft and induces large local conformational rearrangements. Such conformational changes are propagated downward toward the TMD via the palm domain, possibly resulting in outward movement of the TMD and dilation of the ion conduction pore.

PubMed: 37550431
DOI: 10.1038/s41589-023-01401-7

Experimental method

ELECTRON MICROSCOPY (3 Å)