Heptameric structures of two ?-hemolysin mutants imaged with in situ atomic force microscopy
✍ Scribed by Malghani, M.S.; Fang, Ye; Cheley, Stephen; Bayley, Hagan; Yang, Jie
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 289 KB
- Volume
- 44
- Category
- Article
- ISSN
- 1059-910X
No coin nor oath required. For personal study only.
✦ Synopsis
Atomic force microscopy has been used to study self-assembled structures of two ␣-hemolysin mutants. For a mutant (␣HL-H5) that was locked into the prepore state on fluid phase egg-PC membranes, we visualized, for the first time, heptameric prepores and showed that the 7-fold axis in the prepore lies perpendicular to the membrane surface. For another mutant (TCM) with the transmembrane domain, the self-assembled oligomer that assumes the conformation of the fully assembled pore is also a heptamer. These results show that heptamers are the preferred oligomerization state of ␣-hemolysin.