Linked Life Data

9398250

Source:http://linkedlifedata.com/resource/pubmed/id/9398250

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
1998-1-6
pubmed:abstractText
Proteolytic activation, oligomerization, and membrane insertion are three steps that precede channel formation by the bacterial toxin aerolysin. Using attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) and hydrogen-deuterium exchange, the structural changes associated with each step were analyzed. Our results show that activation induces a significant change in secondary structure, characterized by a decrease in random structure and an increase in beta-sheet content. We show that release of the propeptide is essential for this conformational change to occur and that changes are not restricted to the vicinity of the cleavage site but appear to propagate along the molecule. In contrast, subsequent oligomerization of the mature toxin does not involve any change in overall secondary structure but does involve a modification of the tertiary interactions. Finally, insertion of the heptameric complex into dimyristoylphosphatidylcholine vesicles also occurs without major modification of the secondary structure. Studies on the orientations of the secondary structures of the heptamer in the lipid bilayer have also been performed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15224-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel.
pubmed:affiliation
Laboratoire de Chimie Physique des Macromolécules aux Interfaces CP 206/2, Université Libre de Bruxelles, Boulevard du Triomphe, 1050 Bruxelles, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't