5Z1F

Structure of atOSCA3.1 channel

Summary for 5Z1F

• Entry DOI: 10.2210/pdb5z1f/pdb
• EMDB information: 6875
• Descriptor: CSC1-like protein ERD4 (1 entity in total)
• Functional Keywords: osca, tmem63, ion channel, mechanosensitive, membrane protein, osmosensing, metal transport
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 164035.45

Authors

Chen, L.,Zhang, M.,Kang, Y.,Wu, J.X. (deposition date: 2017-12-26, release date: 2018-09-12, Last modification date: 2024-03-27)

Primary citation

Zhang, M.,Wang, D.,Kang, Y.,Wu, J.X.,Yao, F.,Pan, C.,Yan, Z.,Song, C.,Chen, L.
Structure of the mechanosensitive OSCA channels.
Nat. Struct. Mol. Biol., 25:850-858, 2018

PubMed Abstract: Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial physiological processes. Here we show that two members of the OSCA protein family in Arabidopsis thaliana, namely AtOSCA1.1 and AtOSCA3.1, belong to a new class of mechanosensitive ion channels. We solve the structure of the AtOSCA1.1 channel at 3.5-Å resolution and AtOSCA3.1 at 4.8-Å resolution by cryo-electron microscopy. OSCA channels are symmetric dimers that are mediated by cytosolic inter-subunit interactions. Strikingly, they have structural similarity to the mammalian TMEM16 family proteins. Our structural analysis accompanied with electrophysiological studies identifies the ion permeation pathway within each subunit and suggests a conformational change model for activation.

PubMed: 30190597
DOI: 10.1038/s41594-018-0117-6

Experimental method

ELECTRON MICROSCOPY (4.8 Å)