Journal article

Conversion of a transmembrane to a watersoluble protein complex by a single point mutation

Y Tsitrin, CJ Morton, C El Bez, P Paumard, MC Velluz, M Adrian, J Dubochet, MW Parker, S Lanzavecchia, FG van der Goot

Nature Structural & Molecular Biology | NATURE AMERICA INC | Published : 2002


Proteins exist in one of two generally incompatible states: either membrane associated or soluble. Pore-forming proteins are exceptional because they are synthesized as a water-soluble molecule but end up being located in the membrane -- that is, they are nonconstitutive membrane proteins. Here we report the pronounced effect of the single point mutation Y221G of the pore-forming toxin aerolysin. This mutation blocks the hemolytic activity of the toxin but does not affect its initial structure, its ability to bind to cell-surface receptors or its capacity to form heptamers, which constitute the channel-forming unit. The overall structure of the Y221G protein as analyzed by cryo-negative stai..

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