1.A.1.14.6
Bacterial voltage-gated sodium channel, Nav. 3-d crystal structures of vaious conformations are known (4P_3A A-D; 4PA7_A-D; 4P9P_A-D. etc.) (McCusker et al. 2012). It has its internal cavity accessible to the cytoplasmic surface as a result of a bend/rotation about a central residue in the carboxy-terminal TMS that opens the gate to allow entry of hydrated sodium ions. The molecular dynamics of ion transport through the open conformation has been analyzed (Ulmschneider et al. 2013). The C-terminal four helix coiled coil bundle domain couples inactivation with channel opening, depedent on the negatively charged linker region (Bagnéris et al. 2013). A NaVSp1-specific S4-S5 linker peptide induced both an increase in NaVSp1 current density and a negative shift in the activation curve, consistent with the S4-S5 linker stabilizing the open state (Malak et al. 2020).
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Accession Number: | A0L5S6 |
Protein Name: | Ion transport protein |
Length: | 274 |
Molecular Weight: | 30909.00 |
Species: | Magnetococcus sp. (strain MC-1) [156889] |
Number of TMSs: | 4 |
Substrate |
sodium(1+) |
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1: MSRKIRDLIE SKRFQNVITA IIVLNGAVLG LLTDTTLSAS SQNLLERVDQ LCLTIFIVEI
61: SLKIYAYGVR GFFRSGWNLF DFVIVAIALM PAQGSLSVLR TFRIFRVMRL VSVIPTMRRV
121: VQGMLLALPG VGSVAALLTV VFYIAAVMAT NLYGATFPEW FGDLSKSLYT LFQVMTLESW
181: SMGIVRPVMN VHPNAWVFFI PFIMLTTFTV LNLFIGIIVD AMAITKEQEE EAKTGHHQEP
241: ISQTLLHLGD RLDRIEKQLA QNNELLQRQQ PQKK