Autor: |
James Lee, David Tomasek, Thiago MA Santos, Mary D May, Ina Meuskens, Daniel Kahne |
Jazyk: |
angličtina |
Rok vydání: |
2019 |
Předmět: |
|
Zdroj: |
eLife, Vol 8 (2019) |
Druh dokumentu: |
article |
ISSN: |
2050-084X |
DOI: |
10.7554/eLife.49787 |
Popis: |
The β-barrel assembly machine (Bam) complex in Gram-negative bacteria and its counterparts in mitochondria and chloroplasts fold and insert outer membrane β-barrel proteins. BamA, an essential component of the complex, is itself a β-barrel and is proposed to play a central role in assembling other barrel substrates. Here, we map the path of substrate insertion by the Bam complex using site-specific crosslinking to understand the molecular mechanisms that control β-barrel folding and release. We find that the C-terminal strand of the substrate is stably held by BamA and that the N-terminal strands of the substrate are assembled inside the BamA β-barrel. Importantly, we identify contacts between the assembling β-sheet and the BamA interior surface that determine the rate of substrate folding. Our results support a model in which the interior wall of BamA acts as a chaperone to catalyze β-barrel assembly. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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