Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients

Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients

The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate O...

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Autores principales: Antonio N. Calabrese, Bob Schiffrin, Matthew Watson, Theodoros K. Karamanos, Martin Walko, Julia R. Humes, Jim E. Horne, Paul White, Andrew J. Wilson, Antreas C. Kalli, Roman Tuma, Alison E. Ashcroft, David J. Brockwell, Sheena E. Radford
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Science
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Acceso en línea:https://doaj.org/article/2047c9564bc341c98f0fa558c55a100a
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Sumario:The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate OMP binding.

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