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TitleThe inhibition mechanism of the SUR2A-containing K channel by a regulatory helix.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 3608, Year 2023
Publish dateJun 17, 2023
AuthorsDian Ding / Tianyi Hou / Miao Wei / Jing-Xiang Wu / Lei Chen /
PubMed AbstractK channels are metabolic sensors for intracellular ATP/ADP ratios, play essential roles in many physiological processes, and are implicated in a spectrum of pathological conditions. SUR2A-containing ...K channels are metabolic sensors for intracellular ATP/ADP ratios, play essential roles in many physiological processes, and are implicated in a spectrum of pathological conditions. SUR2A-containing K channels differ from other subtypes in their sensitivity to Mg-ADP activation. However, the underlying structural mechanism remains poorly understood. Here we present a series of cryo-EM structures of SUR2A in the presence of different combinations of Mg-nucleotides and the allosteric inhibitor repaglinide. These structures uncover regulatory helix (R helix) on the NBD1-TMD2 linker, which wedges between NBD1 and NBD2. R helix stabilizes SUR2A in the NBD-separated conformation to inhibit channel activation. The competitive binding of Mg-ADP with Mg-ATP to NBD2 mobilizes the R helix to relieve such inhibition, allowing channel activation. The structures of SUR2B in similar conditions suggest that the C-terminal 42 residues of SUR2B enhance the structural dynamics of NBD2 and facilitate the dissociation of the R helix and the binding of Mg-ADP to NBD2, promoting NBD dimerization and subsequent channel activation.
External linksNat Commun / PubMed:37330603 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.8 Å
Structure data

33563

7y1j

EMDB-33563, PDB-7y1j:
Structure of SUR2A in complex with Mg-ATP and repaglinide in the inward-facing conformation.
Method: EM (single particle) / Resolution: 3.0 Å

33564

7y1k

EMDB-33564, PDB-7y1k:
Structure of SUR2A in complex with Mg-ATP, Mg-ADP and repaglinide in the inward-facing conformation
Method: EM (single particle) / Resolution: 3.8 Å

33565

7y1l

EMDB-33565, PDB-7y1l:
Structure of SUR2B in complex with Mg-ATP and repaglinide in the inward-facing conformation
Method: EM (single particle) / Resolution: 3.73 Å

33566

7y1m

EMDB-33566, PDB-7y1m:
Structure of SUR2B in complex with Mg-ATP, Mg-ADP, and repaglinide in the inward-facing conformation
Method: EM (single particle) / Resolution: 3.57 Å

33567

7y1n

EMDB-33567, PDB-7y1n:
Structure of SUR2B in complex with Mg-ATP, Mg-ADP, and repaglinide in the partially occluded state
Method: EM (single particle) / Resolution: 3.61 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-BJX:
Repaglinide / medication*YM / Repaglinide

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / SUR2A / ABC transporter / repaglinide / SUR2B

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