7SIP

Structure of shaker-IR

Summary for 7SIP

• Entry DOI: 10.2210/pdb7sip/pdb
• EMDB information: 25147
• Descriptor: Potassium voltage-gated channel protein Shaker, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: potassium channel, membrane protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 4
• Total formula weight: 302380.10

Authors

Tan, X.,Bae, C.,Stix, R.,Fernandez, A.I.,Huffer, K.,Chang, T.,Jiang, J.,Faraldo-Gomez, J.D.,Swartz, K.J. (deposition date: 2021-10-14, release date: 2022-03-30, Last modification date: 2024-06-05)

Primary citation

Tan, X.F.,Bae, C.,Stix, R.,Fernandez-Marino, A.I.,Huffer, K.,Chang, T.H.,Jiang, J.,Faraldo-Gomez, J.D.,Swartz, K.J.
Structure of the Shaker Kv channel and mechanism of slow C-type inactivation.
Sci Adv, 8:eabm7814-eabm7814, 2022

PubMed Abstract: Voltage-activated potassium (Kv) channels open upon membrane depolarization and proceed to spontaneously inactivate. Inactivation controls neuronal firing rates and serves as a form of short-term memory and is implicated in various human neurological disorders. Here, we use high-resolution cryo-electron microscopy and computer simulations to determine one of the molecular mechanisms underlying this physiologically crucial process. Structures of the activated Shaker Kv channel and of its W434F mutant in lipid bilayers demonstrate that C-type inactivation entails the dilation of the ion selectivity filter and the repositioning of neighboring residues known to be functionally critical. Microsecond-scale molecular dynamics trajectories confirm that these changes inhibit rapid ion permeation through the channel. This long-sought breakthrough establishes how eukaryotic K channels self-regulate their functional state through the plasticity of their selectivity filters.

PubMed: 35302848
DOI: 10.1126/sciadv.abm7814

Experimental method

ELECTRON MICROSCOPY (3 Å)