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TitleCryo-EM structures of pannexin 1 and 3 reveal differences among pannexin isoforms.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 2942, Year 2024
Publish dateApr 5, 2024
AuthorsNazia Hussain / Ashish Apotikar / Shabareesh Pidathala / Sourajit Mukherjee / Ananth Prasad Burada / Sujit Kumar Sikdar / Kutti R Vinothkumar / Aravind Penmatsa /
PubMed AbstractPannexins are single-membrane large-pore channels that release ions and ATP upon activation. Three isoforms of pannexins 1, 2, and 3, perform diverse cellular roles and differ in their pore lining ...Pannexins are single-membrane large-pore channels that release ions and ATP upon activation. Three isoforms of pannexins 1, 2, and 3, perform diverse cellular roles and differ in their pore lining residues. In this study, we report the cryo-EM structure of pannexin 3 at 3.9 Å and analyze its structural differences with pannexin isoforms 1 and 2. The pannexin 3 vestibule has two distinct chambers and a wider pore radius in comparison to pannexins 1 and 2. We further report two cryo-EM structures of pannexin 1, with pore substitutions W74R/R75D that mimic the pore lining residues of pannexin 2 and a germline mutant of pannexin 1, R217H at resolutions of 3.2 Å and 3.9 Å, respectively. Substitution of cationic residues in the vestibule of pannexin 1 results in reduced ATP interaction propensities to the channel. The germline mutant R217H in transmembrane helix 3 (TM3), leads to a partially constricted pore, reduced ATP interaction and weakened voltage sensitivity. The study compares the three pannexin isoform structures, the effects of substitutions of pore and vestibule-lining residues and allosteric effects of a pathological substitution on channel structure and function thereby enhancing our understanding of this vital group of ATP-release channels.
External linksNat Commun / PubMed:38580658 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.91 Å
Structure data

34265

8gtr

EMDB-34265, PDB-8gtr:
CryoEM structure of human Pannexin isoform 3
Method: EM (single particle) / Resolution: 3.91 Å

34266

8gts

EMDB-34266, PDB-8gts:
CryoEM structure of human Pannexin1 with R217H congenital mutation.
Method: EM (single particle) / Resolution: 3.87 Å

34267

8gtt

EMDB-34267, PDB-8gtt:
Cryo-EM structure of human Pannexin1 resembling Pannexin2 pore with W74R/R75Dmutations
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-34268: human Pannexin1
Method: EM (single particle) / Resolution: 3.75 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Pannexins / large pore ion-channels / Pannexin1 / ATP release / large-pore ion channel / large-pore ion channel.

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