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Structure paper

TitleVascular K channel structural dynamics reveal regulatory mechanism by Mg-nucleotides.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 44, Year 2021
Publish dateNov 2, 2021
AuthorsMin Woo Sung / Zhongying Yang / Camden M Driggers / Bruce L Patton / Barmak Mostofian / John D Russo / Daniel M Zuckerman / Show-Ling Shyng /
PubMed AbstractVascular tone is dependent on smooth muscle K channels comprising pore-forming Kir6.1 and regulatory SUR2B subunits, in which mutations cause Cantú syndrome. Unique among K isoforms, they lack ...Vascular tone is dependent on smooth muscle K channels comprising pore-forming Kir6.1 and regulatory SUR2B subunits, in which mutations cause Cantú syndrome. Unique among K isoforms, they lack spontaneous activity and require Mg-nucleotides for activation. Structural mechanisms underlying these properties are unknown. Here, we determined cryogenic electron microscopy structures of vascular K channels bound to inhibitory ATP and glibenclamide, which differ informatively from similarly determined pancreatic K channel isoform (Kir6.2/SUR1). Unlike SUR1, SUR2B subunits adopt distinct rotational "propeller" and "quatrefoil" geometries surrounding their Kir6.1 core. The glutamate/aspartate-rich linker connecting the two halves of the SUR-ABC core is observed in a quatrefoil-like conformation. Molecular dynamics simulations reveal MgADP-dependent dynamic tripartite interactions between this linker, SUR2B, and Kir6.1. The structures captured implicate a progression of intermediate states between MgADP-free inactivated, and MgADP-bound activated conformations wherein the glutamate/aspartate-rich linker participates as mobile autoinhibitory domain, suggesting a conformational pathway toward K channel activation.
External linksProc Natl Acad Sci U S A / PubMed:34711681 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 4.2 Å
Structure data

23864

7mit

EMDB-23864, PDB-7mit:
Vascular KATP channel: Kir6.1 SUR2B propeller-like conformation 1
Method: EM (single particle) / Resolution: 3.4 Å

23880

7mjo

EMDB-23880, PDB-7mjo:
Vascular KATP channel: Kir6.1 SUR2B quatrefoil-like conformation 1
Method: EM (single particle) / Resolution: 4.0 Å

23881

7mjp

EMDB-23881, PDB-7mjp:
Vascular KATP channel: Kir6.1 SUR2B propeller-like conformation 2
Method: EM (single particle) / Resolution: 4.2 Å

23882

7mjq

EMDB-23882, PDB-7mjq:
Vascular KATP channel: Kir6.1 SUR2B quatrefoil-like conformation 2
Method: EM (single particle) / Resolution: 4.2 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

ChemComp-P5S:
O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine

ChemComp-GBM:
5-chloro-N-(2-{4-[(cyclohexylcarbamoyl)sulfamoyl]phenyl}ethyl)-2-methoxybenzamide / medication*YM

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / KATP / potassium channel / vascular

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