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Outer Membrane Targeting of Secretin PulD Protein Relies on Disordered Domain Recognition by a Dedicated Chaperone
Interaction of bacterial outer membrane secretin PulD with its dedicated lipoprotein chaperone PulS relies on a disorder-to-order transition of the chaperone binding (S) domain near the PulD C terminus. PulS interacts with purified S domain to form a 1:1 complex. Circular dichroism, one-dimensional...
Tallennettuna:
| Päätekijät: | , , , , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Society for Biochemistry and Molecular Biology
2011
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3234708/ https://ncbi.nlm.nih.gov/pubmed/21878629 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.279851 |
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