4ZZC

The GLIC pentameric Ligand-Gated Ion Channel open form complexed to xenon

Summary for 4ZZC

• Entry DOI: 10.2210/pdb4zzc/pdb
• Descriptor: Proton-gated ion channel, ACETATE ION, DIUNDECYL PHOSPHATIDYL CHOLINE, ... (8 entities in total)
• Functional Keywords: membrane protein, transport protein
• Biological source: Gloeobacter violaceus (strain PCC 7421)
• Cellular location: Cell inner membrane ; Multi- pass membrane protein : Q7NDN8
• Total number of polymer chains: 5
• Total formula weight: 195525.08

Authors

Sauguet, L.,Fourati, Z.,Prange, T.,Delarue, M.,Colloc'h, N. (deposition date: 2015-05-22, release date: 2016-03-02, Last modification date: 2024-05-08)

Primary citation

Sauguet, L.,Fourati, Z.,Prange, T.,Delarue, M.,Colloc'h, N.
Structural Basis for Xenon Inhibition in a Cationic Pentameric Ligand-Gated Ion Channel.
Plos One, 11:e0149795-e0149795, 2016

PubMed Abstract: GLIC receptor is a bacterial pentameric ligand-gated ion channel whose action is inhibited by xenon. Xenon has been used in clinical practice as a potent gaseous anaesthetic for decades, but the molecular mechanism of interactions with its integral membrane receptor targets remains poorly understood. Here we characterize by X-ray crystallography the xenon-binding sites within both the open and "locally-closed" (inactive) conformations of GLIC. Major binding sites of xenon, which differ between the two conformations, were identified in three distinct regions that all belong to the trans-membrane domain of GLIC: 1) in an intra-subunit cavity, 2) at the interface between adjacent subunits, and 3) in the pore. The pore site is unique to the locally-closed form where the binding of xenon effectively seals the channel. A putative mechanism of the inhibition of GLIC by xenon is proposed, which might be extended to other pentameric cationic ligand-gated ion channels.

PubMed: 26910105
DOI: 10.1371/journal.pone.0149795

Experimental method

X-RAY DIFFRACTION (3.1 Å)