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TitleCryo-EM structure supports a role of AQP7 as a junction protein.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 600, Year 2023
Publish dateFeb 3, 2023
AuthorsPeng Huang / Raminta Venskutonytė / Rashmi B Prasad / Hamidreza Ardalani / Sofia W de Maré / Xiao Fan / Ping Li / Peter Spégel / Nieng Yan / Pontus Gourdon / Isabella Artner / Karin Lindkvist-Petersson /
PubMed AbstractAquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single- ...Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 Å resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic α- and β- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.
External linksNat Commun / PubMed:36737436 / PubMed Central
MethodsEM (single particle)
Resolution2.55 - 3.0 Å
Structure data

15527

8amw

EMDB-15527, PDB-8amw:
AQP7 dimer of tetramers_C1
Method: EM (single particle) / Resolution: 3.0 Å

15528

8amx

EMDB-15528, PDB-8amx:
AQP7 dimer of tetramers_D4
Method: EM (single particle) / Resolution: 2.55 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / membrane channel / octamer / adhesion protein / junction protein

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