5ZX5

3.3 angstrom structure of mouse TRPM7 with EDTA

Summary for 5ZX5

• Entry DOI: 10.2210/pdb5zx5/pdb
• EMDB information: 6975
• Descriptor: Transient receptor potential cation channel subfamily M member 7, CHOLESTEROL HEMISUCCINATE (2 entities in total)
• Functional Keywords: cryoem, truncated mouse trpm7, membrane protein, transferase
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 4
• Total formula weight: 571511.59

Authors

Zhang, J.,Li, Z.,Duan, J.,Li, J.,Hulse, R.E.,Santa-Cruz, A.,Abiria, S.A.,Krapivinsky, G.,Clapham, D.E. (deposition date: 2018-05-18, release date: 2018-10-17, Last modification date: 2024-03-27)

Primary citation

Duan, J.,Li, Z.,Li, J.,Hulse, R.E.,Santa-Cruz, A.,Valinsky, W.C.,Abiria, S.A.,Krapivinsky, G.,Zhang, J.,Clapham, D.E.
Structure of the mammalian TRPM7, a magnesium channel required during embryonic development.
Proc. Natl. Acad. Sci. U.S.A., 115:E8201-E8210, 2018

PubMed Abstract: The transient receptor potential ion channel subfamily M, member 7 (TRPM7), is a ubiquitously expressed protein that is required for mouse embryonic development. TRPM7 contains both an ion channel and an α-kinase. The channel domain comprises a nonselective cation channel with notable permeability to Mg and Zn Here, we report the closed state structures of the mouse TRPM7 channel domain in three different ionic conditions to overall resolutions of 3.3, 3.7, and 4.1 Å. The structures reveal key residues for an ion binding site in the selectivity filter, with proposed partially hydrated Mg ions occupying the center of the conduction pore. In high [Mg], a prominent external disulfide bond is found in the pore helix, which is essential for ion channel function. Our results provide a structural framework for understanding the TRPM1/3/6/7 subfamily and extend the knowledge base upon which to study the diversity and evolution of TRP channels.

PubMed: 30108148
DOI: 10.1073/pnas.1810719115

Experimental method

ELECTRON MICROSCOPY (3.28 Å)