Folding of a bacterial integral outer membrane protein is initiated in the periplasm
The Bam complex promotes the insertion of β-barrel proteins (such as UpaG, a trimeric autotransporter adhesin) into the bacterial outer membrane. Here, Sikdar et al. show that UpaG β-barrel segments fold into a trimeric structure in the periplasm before they interact with the Bam complex.
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2017-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-01246-4 |
| Summary: | The Bam complex promotes the insertion of β-barrel proteins (such as UpaG, a trimeric autotransporter adhesin) into the bacterial outer membrane. Here, Sikdar et al. show that UpaG β-barrel segments fold into a trimeric structure in the periplasm before they interact with the Bam complex. |
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| ISSN: | 2041-1723 |