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...

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Hlavní autoři: Nickerson, Nicholas N., Tosi, Tommaso, Dessen, Andréa, Baron, Bruno, Raynal, Bertrand, England, Patrick, Pugsley, Anthony P.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2011
Témata:
Microbiology
On-line přístup: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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