5YUA

Crystal structure of voltage-gated sodium channel NavAb in high-pH condition

Summary for 5YUA

• Entry DOI: 10.2210/pdb5yua/pdb
• Descriptor: Ion transport protein, CALCIUM ION, DODECYL-BETA-D-MALTOSIDE, ... (6 entities in total)
• Functional Keywords: ion channel, membrane protein
• Biological source: Arcobacter butzleri
• Total number of polymer chains: 1
• Total formula weight: 37149.04

Authors

Irie, K.,Shimomura, T.,Fujiyoshi, Y. (deposition date: 2017-11-21, release date: 2017-12-27, Last modification date: 2023-11-22)

Primary citation

Irie, K.,Haga, Y.,Shimomura, T.,Fujiyoshi, Y.
Structural insight on the voltage dependence of prokaryotic voltage gated sodium channel NavAb.
FEBS Lett., 2017

PubMed Abstract: Voltage-gated sodium channels are crucial for electro-signalling in living systems. Analysis of the molecular mechanism requires both fine electrophysiological evaluation and high-resolution channel structures. Here, we optimized a dual expression system of NavAb, which is a well-established standard of prokaryotic voltage-gated sodium channels, for E. coli and insect cells using a single plasmid vector to analyse high-resolution protein structures and measure large ionic currents. Using this expression system, we evaluated the voltage dependence and determined the crystal structures of NavAb wild-type and two mutants, E32Q and N49K, whose voltage dependence were positively shifted and essential interactions were lost in voltage sensor domain. The structural and functional comparison elucidated the molecular mechanisms of the voltage dependence of prokaryotic voltage-gated sodium channels.

PubMed: 29274127
DOI: 10.1002/1873-3468.12955

Experimental method

X-RAY DIFFRACTION (2.8008556672 Å)