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TitleCryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateJan 16, 2017
AuthorsGregory M Martin / Craig Yoshioka / Emily A Rex / Jonathan F Fay / Qing Xie / Matthew R Whorton / James Z Chen / Show-Ling Shyng /
PubMed AbstractK channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic β-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of ...K channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic β-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of antidiabetic sulfonylureas. Here, we used cryo-EM to elucidate structural basis of channel assembly and gating. The structure, determined in the presence of ATP and the sulfonylurea glibenclamide, at ~6 Å resolution reveals a closed Kir6.2 tetrameric core with four peripheral SUR1s each anchored to a Kir6.2 by its N-terminal transmembrane domain (TMD0). Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP binding to enhance Kir6.2 sensitivity to both. The SUR1-ABC core is found in an unusual inward-facing conformation whereby the two nucleotide binding domains are misaligned along a two-fold symmetry axis, revealing a possible mechanism by which glibenclamide inhibits channel activity.
External linksElife / PubMed:28092267 / PubMed Central
MethodsEM (single particle)
Resolution6.3 Å
Structure data

EMDB-8470, PDB-5twv:
Cryo-EM structure of the pancreatic ATP-sensitive K+ channel SUR1/Kir6.2 in the presence of ATP and glibenclamide
Method: EM (single particle) / Resolution: 6.3 Å

Chemicals

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

Source
  • rattus norvegicus (Norway rat)
  • cricetus cricetus (black-bellied hamster)
KeywordsAbcc8 protein, rat / Adenosine Triphosphate / Cryoelectron Microscopy / Glyburide / Humans / Kir6.2 channel / Models, Molecular / Potassium Channels, Inwardly Rectifying / Protein Conformation / Protein Multimerization / Sulfonylurea Receptors / TRANSPORT PROTEIN / katp / kir6.2 / sur1 / potassium channel

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