Figures
Yeast aquaporin gating.
An article in the June issue of PLoS Biology reports the crystal structure of a gated aquaporin from yeast at the highest resolution so far obtained for a membrane protein (see Fischer et al., e1000130). At this resolution it is possible to view the specific orientation of water molecules as they pass through the channel and to see how the co-transport of protons is excluded. The structure reveals that yeast aquaporins are gated, providing an energetically economical solution to the need to respond to the numerous stresses associated with rapidly changing environments, aiding the organism's quest to survive.
Image Credit: Urszula Kosinska-Eriksson, Gerhard Fischer (University of Gothenburg).
Citation: (2009) PLoS Biology Issue Image | Vol. 7(6) June 2009. PLoS Biol 7(6): ev07.i06. https://doi.org/10.1371/image.pbio.v07.i06
Published: June 30, 2009
Copyright: © 2009 Fischer et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
An article in the June issue of PLoS Biology reports the crystal structure of a gated aquaporin from yeast at the highest resolution so far obtained for a membrane protein (see Fischer et al., e1000130). At this resolution it is possible to view the specific orientation of water molecules as they pass through the channel and to see how the co-transport of protons is excluded. The structure reveals that yeast aquaporins are gated, providing an energetically economical solution to the need to respond to the numerous stresses associated with rapidly changing environments, aiding the organism's quest to survive.
Image Credit: Urszula Kosinska-Eriksson, Gerhard Fischer (University of Gothenburg).