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Structure paper

TitleCryo-EM structures of the small-conductance Ca-activated K2.2 channel.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 3690, Year 2025
Publish dateApr 17, 2025
AuthorsYoung-Woo Nam / Dohyun Im / Ana Santa Cruz Garcia / Marios L Tringides / Hai Minh Nguyen / Yan Liu / Razan Orfali / Alena Ramanishka / Grigore Pintilie / Chih-Chia Su / Meng Cui / Diomedes E Logothetis / Edward W Yu / Heike Wulff / K George Chandy / Miao Zhang /
PubMed AbstractSmall-conductance Ca-activated K (K2.1-K2.3) channels modulate neuronal and cardiac excitability. We report cryo-electron microscopy structures of the K2.2 channel in complex with calmodulin and Ca, ...Small-conductance Ca-activated K (K2.1-K2.3) channels modulate neuronal and cardiac excitability. We report cryo-electron microscopy structures of the K2.2 channel in complex with calmodulin and Ca, alone or bound to two small molecule inhibitors, at 3.18, 3.50, 2.99 and 2.97 angstrom resolution, respectively. Extracellular S3-S4 loops in β-hairpin configuration form an outer canopy over the pore with an aromatic box at the canopy's center. Each S3-S4 β-hairpin is tethered to the selectivity filter in the neighboring subunit by inter-subunit hydrogen bonds. This hydrogen bond network flips the aromatic residue (Tyr362) in the filter's GYG signature by 180°, causing the outer selectivity filter to widen and water to enter the filter. Disruption of the tether by a mutation narrows the outer selectivity filter, realigns Tyr362 to the position seen in other K channels, and significantly increases unitary conductance. UCL1684, a mimetic of the bee venom peptide apamin, sits atop the canopy and occludes the opening in the aromatic box. AP14145, an analogue of a therapeutic for atrial fibrillation, binds in the central cavity below the selectivity filter and induces closure of the inner gate. These structures provide a basis for understanding the small unitary conductance and pharmacology of K2.x channels.
External linksNat Commun / PubMed:40246884 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.62 Å
Structure data

42911

8v2g

EMDB-42911, PDB-8v2g:
Cryo-EM structure of the KCa2.2 channel in apo state
Method: EM (single particle) / Resolution: 3.18 Å

42914

8v2h

EMDB-42914, PDB-8v2h:
Cryo-EM structure of the KCa2.2 channel bound to inhibitor AP14145.
Method: EM (single particle) / Resolution: 3.1 Å

42947

8v3g

EMDB-42947, PDB-8v3g:
Cryo-EM structure of the KCa2.2 channel with inhibitor UCL 1684.
Method: EM (single particle) / Resolution: 3.1 Å

48088

9eio

EMDB-48088, PDB-9eio:
Cryo-EM structure of the mutant KCa2.2_F244S channel
Method: EM (single particle) / Resolution: 3.62 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER


ChemComp, No image

ChemComp-Y7Z:
Unknown entry

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / Ion channel / Calmodulin binding protein / TRANSPORT PROTEIN/INHIBITOR / TRANSPORT PROTEIN-INHIBITOR complex / Calmodulin binding protein. Membrane protein

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