RRC ID 19114
Author Irie K, Shimomura T, Fujiyoshi Y.
Title The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate.
Journal Nat Commun
Abstract Most tetrameric channels have cytosolic domains to regulate their functions, including channel inactivation. Here we show that the cytosolic C-terminal region of NavSulP, a prokaryotic voltage-gated sodium channel cloned from Sulfitobacter pontiacus, accelerates channel inactivation. The crystal structure of the C-terminal region of NavSulP grafted into the C-terminus of a NaK channel revealed that the NavSulP C-terminal region forms a four-helix bundle. Point mutations of the residues involved in the intersubunit interactions of the four-helix bundle destabilized the tetramer of the channel and reduced the inactivation rate. The four-helix bundle was directly connected to the inner helix of the pore domain, and a mutation increasing the rigidity of the inner helix also reduced the inactivation rate. These findings suggest that the NavSulP four-helix bundle has important roles not only in stabilizing the tetramer, but also in accelerating the inactivation rate, through promotion of the conformational change of the inner helix.
Volume 3
Pages 793
Published 2012-4-24
DOI 10.1038/ncomms1797
PII ncomms1797
PMID 22531178
PMC PMC3337986
MeSH Amino Acid Motifs Amino Acid Sequence Bacterial Proteins / chemistry* Bacterial Proteins / genetics Bacterial Proteins / metabolism* Crystallography, X-Ray Kinetics Models, Molecular Molecular Sequence Data Phylogeny Point Mutation Protein Multimerization Protein Structure, Tertiary Rhodobacteraceae / chemistry Rhodobacteraceae / classification Rhodobacteraceae / genetics Rhodobacteraceae / metabolism* Sodium Channels / chemistry* Sodium Channels / genetics Sodium Channels / metabolism*
IF 12.353
Times Cited 12
General Microbes JCM 21789