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• W2022347002 abstract "We analyzed the structure of aquaporin-1 (AQP1) by electron crystallography. The scaffold of the AQP1 molecule was formed by two helical bundles of 1-3 and 4-6. These two helical bundles are unusual in that the three helices form a roughly linear arrangement but not according to their position in the primary structure, that is, 1-2-3 and 4-5-6, but the first helix of each bundle is sandwiched between the other two helices of the bundle, that is, 2-1-3 and 5-4-6. Two helices of each bundle, helices 1 and 2 of the first bundle and helices 4 and 5 of the second bundle, run almost parallel to each other, tilting roughly in the same direction in the membrane. However, the third helix of the first bundle, helix 3, is oriented perpendicular to the axis defined by the first two helices of the bundle, and the same is found for helix 6 in the second helical bundle. The short helix HB from the first AQP1 repeat strongly interacts with transmembrane helix 6 from the second AQP1 repeat, while the short helix HE from the second AQP1 repeat interacts with transmembrane helix 3 from the first AQP1 repeat. This cross-interaction leads to an intimate link of the two protein halves. After helix 2, which crosses the membrane adjacent to helix 1, near the fourfold axis of the AQP1 tetramer, loop B, immediately folds back into the membrane positioning its NPA motif is in the middle between the two helical bundles 1-3 and 4-6, close to the center of the lipid bilayer. After the NPA motif, loop B forms the short α-helix HB, which runs close to helix 6 of the second AQP1 repeat and brings the polypeptide chain back to the cytoplasmic surface. The remainder of loop B forms the cytoplasmic connection to helix 3, which crosses the membrane adjacent to helix 1, on the opposite side from helix 2. Helix 3 is the last structural element of the first AQP1 repeat that terminates on the extracellular surface. The second AQP1 repeat adopts essentially the same fold as the first and the two repeats are connected by loop C. The analyzed structure reveals key amino acid residues that are conserved throughout the AQP family and stabilize a novel and unusual fold of AQP1. The water pathway is lined with conserved hydrophobic residues that serve for the rapid water transport, whereas the water selectivity is due to a constriction of the small pore diameter over a length of only one amino acid residue. The structure enables us to theorize that it is a molecular mechanism for the effective blocking of proton transport while maintaining a high water permeability, thus offering an explanation of a long-standing puzzle." @default.
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• W2022347002 date "2001-08-01" @default.
• W2022347002 modified "2023-09-25" @default.
• W2022347002 title "Molecular basis of water selectivity on aquaporin-1" @default.
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• W2022347002 doi "https://doi.org/10.1046/j.1523-1755.2001.00821-5.x" @default.
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