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Slow conformational dynamics of an endonuclease persist in its complex with its natural protein inhibitor.

The bacterial toxin colicin E9 is secreted by producing Escherichia coli cells with its 9.5 kDa inhibitor protein Im9 bound tightly to its 14.5 kDa C-terminal DNase domain. Double- and triple-resonance NMR spectra of the isolated DNase domain uniformly labeled with 13C/15N bound to unlabeled Im9 con...

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Main Authors: Whittaker, S. B., Czisch, M., Wechselberger, R., Kaptein, R., Hemmings, A. M., James, R., Kleanthous, C., Moore, G. R.
Formato: Artigo
Idioma:Inglês
Publicado: Cold Spring Harbor Laboratory Press 2000
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144623/
https://ncbi.nlm.nih.gov/pubmed/10794413
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