4H37

Crystal structure of a voltage-gated K+ channel pore domain in a closed state in lipid membranes

Summary for 4H37

• Entry DOI: 10.2210/pdb4h37/pdb
• Related: 4H33
• Descriptor: Lmo2059 protein, POTASSIUM ION (2 entities in total)
• Functional Keywords: module, pore module, ion channel, membrane, membrane protein
• Biological source: Listeria monocytogenes
• Total number of polymer chains: 2
• Total formula weight: 31279.26

Authors

Santos, J.S.,Asmar-Rovira, G.A.,Han, G.W.,Liu, W.,Syeda, R.,Cherezov, V.,Baker, K.A.,Stevens, R.C.,Montal, M. (deposition date: 2012-09-13, release date: 2012-11-07, Last modification date: 2023-09-20)

Primary citation

Santos, J.S.,Asmar-Rovira, G.A.,Han, G.W.,Liu, W.,Syeda, R.,Cherezov, V.,Baker, K.A.,Stevens, R.C.,Montal, M.
Crystal Structure of a Voltage-gated K+ Channel Pore Module in a Closed State in Lipid Membranes.
J.Biol.Chem., 287:43063-43070, 2012

PubMed Abstract: Voltage-gated K(+) channels underlie the electrical excitability of cells. Each subunit of the functional tetramer consists of the tandem fusion of two modules, an N-terminal voltage-sensor and a C-terminal pore. To investigate how sensor coupling to the pore generates voltage-dependent channel opening, we solved the crystal structure and characterized the function of a voltage-gated K(+) channel pore in a lipid membrane. The structure of a functional channel in a membrane environment at 3.1 Å resolution establishes an unprecedented connection between channel structure and function. The structure is unique in delineating an ion-occupied ready to conduct selectivity filter, a confined aqueous cavity, and a closed activation gate, embodying a dynamic entity trapped in an unstable closed state.

PubMed: 23095758
DOI: 10.1074/jbc.M112.415091

Experimental method

X-RAY DIFFRACTION (3.35 Å)