Gast ::
| Hauptseite > Publikationsdatenbank > An RTX toxin transporters tether ist substrate prior to secretion via the unique function of ist N- terminal domain |
| Hauptseite > Publikationsdatenbank > An RTX toxin transporters tether ist substrate prior to secretion via the unique function of ist N- terminal domain |
| Journal Article | PreJuSER-23152 |
; ; ; ; ;
2012
Elsevier Science
London [u.a.]
This record in other databases: 
Please use a persistent id in citations: doi:10.1016/j.str.2012.08.005
Abstract: Type 1 secretion systems (T1SS) catalyze the one step protein transport across the membranes of Gram-negative bacteria and are composed of an outer membrane protein, a membrane fusion protein and an ABC transporter. The ABC transporter consists of the canonical nucleotide binding and transmembrane domains. For the toxin hemolysin A (HlyA), the ABC transporter HlyB carries an additional, N-terminal domain sharing about 40% homology to C39 peptidases, but this "C39-like domain" (CLD) is suggested to feature another, yet unknown function. Our functional and structural analysis demonstrates that the CLD is essential for secretion and that it specifically interacts with the unfolded state of HlyA. We determined the nuclear magnetic resonance structure of the CLD as well as the substrate-binding region within the CLD. This mode of action, represents a mechanism within T1SS and answers the question, how a large and unfolded substrate is protected inside the cells during secretion.
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz
; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
|
The record appears in these collections: |