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TitleStructural analysis of the water channel AQP2 by single-particle cryo-EM.
Journal, issue, pagesJ Struct Biol, Vol. 215, Issue 3, Page 107984, Year 2023
Publish dateJun 12, 2023
AuthorsAkiko Kamegawa / Shota Suzuki / Hiroshi Suzuki / Kouki Nishikawa / Nobutaka Numoto / Yoshinori Fujiyoshi /
PubMed AbstractWater channels, which are small membrane proteins almost entirely buried in lipid membranes, are challenging research targets for single-particle cryo-electron microscopy (cryo-EM), a powerful ...Water channels, which are small membrane proteins almost entirely buried in lipid membranes, are challenging research targets for single-particle cryo-electron microscopy (cryo-EM), a powerful technique routinely used to determine the structures of membrane proteins. Because the single-particle method enables structural analysis of a whole protein with flexible parts that interfere with crystallization, we have focused our efforts on analyzing water channel structures. Here, utilizing this system, we analyzed the structure of full-length aquaporin-2 (AQP2), a primary regulator of vasopressin-dependent reabsorption of water at the renal collecting ducts. The 2.9 Å resolution map revealed a cytoplasmic extension of the cryo-EM density that was presumed to be the highly flexible C-terminus at which the localization of AQP2 is regulated in the renal collecting duct cells. We also observed a continuous density along the common water pathway inside the channel pore and lipid-like molecules at the membrane interface. Observations of these constructions in the AQP2 structure analyzed without any fiducial markers (e.g., a rigidly bound antibody) indicate that single-particle cryo-EM will be useful for investigating water channels in native states as well as in complexes with chemical compounds.
External linksJ Struct Biol / PubMed:37315821
MethodsEM (single particle)
Resolution2.89 Å
Structure data

29934

8gcl

EMDB-29934, PDB-8gcl:
Cryo-EM structure of hAQP2 in DDM
Method: EM (single particle) / Resolution: 2.89 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / channel

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