5hkt | pdb_00005hkt

Bacterial sodium channel pore domain, high bromide

spinqualitylabelsall models 5hkt, resolution 3.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hkt is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5hj8, 5hk6, 5hk7, 5hkd, 5hku Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed Voltage-gated ion channels (VGICs) are outfitted with diverse cytoplasmic domains that impact function. To examine how such elements may affect VGIC behavior, we addressed how the bacterial voltage-gated sodium channel (BacNaV) C-terminal cytoplasmic domain (CTD) affects function. Our studies show that the BacNaV CTD exerts a profound influence on gating through a temperature-dependent unfolding transition in a discrete cytoplasmic domain, the neck domain, proximal to the pore. Structural and functional studies establish that the BacNaV CTD comprises a bi-partite four-helix bundle that bears an unusual hydrophilic core whose integrity is central to the unfolding mechanism and that couples directly to the channel activation gate. Together, our findings define a general principle for how the widespread four-helix bundle cytoplasmic domain architecture can control VGIC responses, uncover a mechanism underlying the diverse BacNaV voltage dependencies, and demonstrate that a discrete domain can encode the temperature-dependent response of a channel. Unfolding of a Temperature-Sensitive Domain Controls Voltage-Gated Channel Activation.,Arrigoni C, Rohaim A, Shaya D, Findeisen F, Stein RA, Nurva SR, Mishra S, Mchaourab HS, Minor DL Jr Cell. 2016 Feb 25;164(5):922-36. doi: 10.1016/j.cell.2016.02.001. PMID:26919429 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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