Heptameric structures of two alpha-hemolysin mutants imaged with in situ atomic force microscopy.

Abstract:

:Atomic force microscopy has been used to study self-assembled structures of two alpha-hemolysin mutants. For a mutant (alphaHL-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 alpha-hemolysin.

journal_name

Microsc Res Tech

authors

Malghani MS,Fang Y,Cheley S,Bayley H,Yang J

doi

10.1002/(SICI)1097-0029(19990301)44:5<353::AID-JEM

keywords:

subject

Has Abstract

pub_date

1999-03-01 00:00:00

pages

353-6

issue

5

eissn

1059-910X

issn

1097-0029

pii

10.1002/(SICI)1097-0029(19990301)44:5<353::AID-JEM

journal_volume

44

pub_type

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