7N5E

Structure of Mechanosensitive Ion Channel Flycatcher1 in GDN

Summary for 7N5E

• Entry DOI: 10.2210/pdb7n5e/pdb
• EMDB information: 24186 24187 24188 24189
• Descriptor: Mechanosensitive ion channel Flycatcher1, PALMITIC ACID (2 entities in total)
• Functional Keywords: mechanically activated ion channel, membrane protein
• Biological source: Dionaea muscipula
• Total number of polymer chains: 7
• Total formula weight: 609496.63

Authors

Jojoa-Cruz, S.,Saotome, K.,Lee, W.H.,Patapoutian, A.,Ward, A.B. (deposition date: 2021-06-05, release date: 2022-02-16, Last modification date: 2024-05-29)

Primary citation

Jojoa-Cruz, S.,Saotome, K.,Tsui, C.C.A.,Lee, W.H.,Sansom, M.S.P.,Murthy, S.E.,Patapoutian, A.,Ward, A.B.
Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1.
Nat Commun, 13:850-850, 2022

PubMed Abstract: Flycatcher1 (FLYC1), a MscS homolog, has recently been identified as a candidate mechanosensitive (MS) ion channel involved in Venus flytrap prey recognition. FLYC1 is a larger protein and its sequence diverges from previously studied MscS homologs, suggesting it has unique structural features that contribute to its function. Here, we characterize FLYC1 by cryo-electron microscopy, molecular dynamics simulations, and electrophysiology. Akin to bacterial MscS and plant MSL1 channels, we find that FLYC1 central core includes side portals in the cytoplasmic cage that regulate ion preference and conduction, by identifying critical residues that modulate channel conductance. Topologically unique cytoplasmic flanking regions can adopt 'up' or 'down' conformations, making the channel asymmetric. Disruption of an up conformation-specific interaction severely delays channel deactivation by 40-fold likely due to stabilization of the channel open state. Our results illustrate novel structural features and likely conformational transitions that regulate mechano-gating of FLYC1.

PubMed: 35165281
DOI: 10.1038/s41467-022-28511-5

Experimental method

ELECTRON MICROSCOPY (2.8 Å)