1.A.1.14.7 Tetrameric 6 TMS subunit Na+ channel protein, NaV. Two low resolution cyroEM structures revealed two conformations
reconstituted in lipid bilayers (Tsai et al. 2013). Despite a voltage sensor arrangement
identical with that in the activated form, Tsai et al. 2013 observed two distinct pore
domain structures: a prominent form with a relatively open inner gate,
and a closed inner-gate conformation similar to the first prokaryotic Nav structure. Structural differences, together with mutational and
electrophysiological analyses, indicated that widening of the inner gate
was dependent on interactions among the S4-S5 linker, the N-terminal
part of S5 and its adjoining part in S6, and on interhelical repulsion
by a negatively charged C-terminal region subsequent to S6 (Tsai et al. 2013).
|
Accession Number: | F5L478 |
Protein Name: | Ion transport protein |
Length: | 298 |
Molecular Weight: | 34442.00 |
Species: | Caldalkalibacillus thermarum TA2.A1 [986075] |
Number of TMSs: | 5 |
Substrate |
sodium(1+) |
---|
1: MSHIHERHSQ LKHPIEAWCD WLVNHPRFTS AIIVLIVINA IVVGMETYPG IYQPYQDWFY
61: LIDRMILWVF TAEIILKLVA TRPRYHFFKD SWNVFDFLIV ASGHLFVGAQ FVTVLRVLRV
121: LRLLRAVTVI PSLRRLVSAL LYTIPSLGNI MLLMGLIFYI FGVMGTFLFR DVAPEYFGSL
181: HLSLITLFQV VTLESWASGI MRPIMAEVFW SWIYFVAFIL VGTFVIFNLF VGVIVSNVER
241: AETEDAEQEE GQREERQGLF EGDGSSVSAE EIAKLRQEIK ELRQLLKELK DHHSQSST