Model-based prediction of the alpha-hemolysin structure in the hexameric state.

ABSTRACT: The alpha-hemolysin toxin self-assembles in lipid bilayers to form water-filled pores. In recent years, alpha-hemolysin has received great attention, mainly due to its possible usage as a sensing element. We measured the ion currents through single alpha-hemolysin channels and confirmed the presence of two different subpopulations of channels with conductance levels of 465 +/- 30 pS and 280 +/- 30 pS. Different oligomerization states could be responsible for these two conductances. In fact, a heptameric structure of the channel was revealed by x-ray crystallography, whereas atomic force microscopy revealed a hexameric structure. Due to the low resolution of atomic force microscopy the atomic details of the hexameric structure are still unknown, and are here predicted by computational metho

SUBMITTER: Furini S 

PROVIDER: S-EPMC2517045 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature