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TitleThe Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateFeb 12, 2020
AuthorsKevin Michalski / Johanna L Syrjanen / Erik Henze / Julia Kumpf / Hiro Furukawa / Toshimitsu Kawate /
PubMed AbstractPannexins are large-pore forming channels responsible for ATP release under a variety of physiological and pathological conditions. Although predicted to share similar membrane topology with other ...Pannexins are large-pore forming channels responsible for ATP release under a variety of physiological and pathological conditions. Although predicted to share similar membrane topology with other large-pore forming proteins such as connexins, innexins, and LRRC8, pannexins have minimal sequence similarity to these protein families. Here, we present the cryo-EM structure of a frog pannexin 1 (Panx1) channel at 3.0 Å. We find that Panx1 protomers harbor four transmembrane helices similar in arrangement to other large-pore forming proteins but assemble as a heptameric channel with a unique constriction formed by Trp74 in the first extracellular loop. Mutating Trp74 or the nearby Arg75 disrupt ion selectivity, whereas altering residues in the hydrophobic groove formed by the two extracellular loops abrogates channel inhibition by carbenoxolone. Our structural and functional study establishes the extracellular loops as important structural motifs for ion selectivity and channel inhibition in Panx1.
External linksElife / PubMed:32048993 / PubMed Central
MethodsEM (single particle)
Resolution3.02 Å
Structure data

21150

6vd7

EMDB-21150, PDB-6vd7:
Cryo-EM structure of Xenopus tropicalis pannexin 1 channel
Method: EM (single particle) / Resolution: 3.02 Å

Source
  • xenopus tropicalis (tropical clawed frog)
KeywordsTRANSPORT PROTEIN / channel / ATP release / heptamer

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