6BCL

cryo-EM structure of TRPM4 in apo state with long coiled coil at 3.5 angstrom resolution

Summary for 6BCL

• Entry DOI: 10.2210/pdb6bcl/pdb
• Related: 6BCJ 6BCO 6BCQ
• EMDB information: 7081 7082 7083 7085
• Descriptor: Transient receptor potential cation channel subfamily M member 4, SODIUM ION (2 entities in total)
• Functional Keywords: ion channel, transport protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 4
• Total formula weight: 563737.48

Authors

Guo, J.,She, J.,Chen, Q.,Bai, X.,Jiang, Y. (deposition date: 2017-10-20, release date: 2017-12-13, Last modification date: 2024-10-09)

Primary citation

Guo, J.,She, J.,Zeng, W.,Chen, Q.,Bai, X.C.,Jiang, Y.
Structures of the calcium-activated, non-selective cation channel TRPM4.
Nature, 552:205-209, 2017

PubMed Abstract: TRPM4 is a calcium-activated, phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P) -modulated, non-selective cation channel that belongs to the family of melastatin-related transient receptor potential (TRPM) channels. Here we present the electron cryo-microscopy structures of the mouse TRPM4 channel with and without ATP. TRPM4 consists of multiple transmembrane and cytosolic domains, which assemble into a three-tiered architecture. The N-terminal nucleotide-binding domain and the C-terminal coiled-coil participate in the tetrameric assembly of the channel; ATP binds at the nucleotide-binding domain and inhibits channel activity. TRPM4 has an exceptionally wide filter but is only permeable to monovalent cations; filter residue Gln973 is essential in defining monovalent selectivity. The S1-S4 domain and the post-S6 TRP domain form the central gating apparatus that probably houses the Ca- and PtdIns(4,5)P-binding sites. These structures provide an essential starting point for elucidating the complex gating mechanisms of TRPM4 and reveal the molecular architecture of the TRPM family.

PubMed: 29211714
DOI: 10.1038/nature24997

Experimental method

ELECTRON MICROSCOPY (3.54 Å)