7w7s | pdb_00007w7s

High resolution structure of a fish aquaporin reveals a novel extracellular fold.

spinqualitylabelsall models 7w7s, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7w7s is a 1 chain structure with sequence from Anabas testudineus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1K561_ANATE Publication Abstract from PubMed Aquaporins are protein channels embedded in the lipid bilayer in cells from all organisms on earth that are crucial for water homeostasis. In fish, aquaporins are believed to be important for osmoregulation; however, the molecular mechanism behind this is poorly understood. Here, we present the first structural and functional characterization of a fish aquaporin; cpAQP1aa from the fresh water fish climbing perch (<i>Anabas testudineus</i>), a species that is of high osmoregulatory interest because of its ability to spend time in seawater and on land. These studies show that cpAQP1aa is a water-specific aquaporin with a unique fold on the extracellular side that results in a constriction region. Functional analysis combined with molecular dynamic simulations suggests that phosphorylation at two sites causes structural perturbations in this region that may have implications for channel gating from the extracellular side. High-resolution structure of a fish aquaporin reveals a novel extracellular fold.,Zeng J, Schmitz F, Isaksson S, Glas J, Arbab O, Andersson M, Sundell K, Eriksson LA, Swaminathan K, Tornroth-Horsefield S, Hedfalk K Life Sci Alliance. 2022 Oct 13;5(12):e202201491. doi: 10.26508/lsa.202201491. PMID:36229063 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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