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J Struct Biol. 1999 Dec 1;128(1):34-43.

The structure of aquaporin-1 at 4.5-A resolution reveals short alpha-helices in the center of the monomer.

Author information

1
Faculty of Science, Kyoto University, Kyoto, Japan.

Abstract

Aquaporin-1 is a water channel found in mammalian red blood cells that is responsible for high water permeability of its membrane. Our electron crystallographic analysis of the three-dimensional structure of aquaporin-1 at 4.5-A resolution confirms the previous finding that each subunit consists of a right-handed bundle of six highly tilted transmembrane helices that surround a central X-shaped structure. In our new potential map, the rod-like densities for the transmembrane helices show helically arranged protrusions, indicating the positions of side chains. Thus, in addition to the six transmembrane helices, observation of helically arranged side-chain densities allowed the identification of two short alpha-helices representing the two branches of the central X-shaped structure that extend to the extracellular and cytoplasmic membrane surfaces. The other two branches are believed to be loops connecting the short alpha-helix to a neighboring transmembrane helix. A pore found close to the center of the aquaporin-1 monomer is suggested to be the course of water flow with implications for the water selectivity.

PMID:
10600556
DOI:
10.1006/jsbi.1999.4177
[Indexed for MEDLINE]

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