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7PGI

NaVAb1p (bicelles)

Summary for 7PGI
Entry DOI10.2210/pdb7pgi/pdb
Related7PG8 7PGF 7PGG 7PGP
DescriptorIon transport protein, ACETATE ION, SODIUM ION, ... (4 entities in total)
Functional Keywordsion channel membrane protein transport protein antibody complex, membrane protein
Biological sourceAlcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Total number of polymer chains8
Total formula weight136044.97
Authors
Lolicato, M.,Arrigoni, C. (deposition date: 2021-08-14, release date: 2022-06-08, Last modification date: 2024-01-31)
Primary citationArrigoni, C.,Lolicato, M.,Shaya, D.,Rohaim, A.,Findeisen, F.,Fong, L.K.,Colleran, C.M.,Dominik, P.,Kim, S.S.,Schuermann, J.P.,DeGrado, W.F.,Grabe, M.,Kossiakoff, A.A.,Minor Jr., D.L.
Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.
Nat.Struct.Mol.Biol., 29:537-548, 2022
Cited by
PubMed Abstract: Every voltage-gated ion channel (VGIC) has a pore domain (PD) made from four subunits, each comprising an antiparallel transmembrane helix pair bridged by a loop. The extent to which PD subunit structure requires quaternary interactions is unclear. Here, we present crystal structures of a set of bacterial voltage-gated sodium channel (BacNa) 'pore only' proteins that reveal a surprising collection of non-canonical quaternary arrangements in which the PD tertiary structure is maintained. This context-independent structural robustness, supported by molecular dynamics simulations, indicates that VGIC-PD tertiary structure is independent of quaternary interactions. This fold occurs throughout the VGIC superfamily and in diverse transmembrane and soluble proteins. Strikingly, characterization of PD subunit-binding Fabs indicates that non-canonical quaternary PD conformations can occur in full-length VGICs. Together, our data demonstrate that the VGIC-PD is an autonomously folded unit. This property has implications for VGIC biogenesis, understanding functional states, de novo channel design, and VGIC structural origins.
PubMed: 35655098
DOI: 10.1038/s41594-022-00775-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.638 Å)
Structure validation

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