8AMX

AQP7 dimer of tetramers_D4

Summary for 8AMX

• Entry DOI: 10.2210/pdb8amx/pdb
• EMDB information: 15528
• Descriptor: Aquaporin-7 (2 entities in total)
• Functional Keywords: membrane channel, octamer, adhesion protein, junction protein, membrane protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 8
• Total formula weight: 298115.16

Authors

Huang, P.,Venskutonyte, R.,Fan, X.,Li, P.,Yan, N.,Gourdon, P.,Lindkvist-Petersson, K. (deposition date: 2022-08-04, release date: 2023-02-15, Last modification date: 2024-07-24)

Primary citation

Huang, P.,Venskutonyte, R.,Prasad, R.B.,Ardalani, H.,de Mare, S.W.,Fan, X.,Li, P.,Spegel, P.,Yan, N.,Gourdon, P.,Artner, I.,Lindkvist-Petersson, K.
Cryo-EM structure supports a role of AQP7 as a junction protein.
Nat Commun, 14:600-600, 2023

PubMed Abstract: 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.

PubMed: 36737436
DOI: 10.1038/s41467-023-36272-y

Experimental method

ELECTRON MICROSCOPY (2.55 Å)