Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer

Ming Tang, Anna E. Nesbitt, Lindsay J. Sperling, Deborah A. Berthold, Charles D. Schwieters, Robert B. Gennis, Chad M. Rienstra

Research output: Contribution to journalArticlepeer-review


The integral membrane protein DsbB in Escherichia coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. We have developed a high-resolution structural model by combining experimental X-ray and solid-state NMR with molecular dynamics (MD) simulations. We embedded the high-resolution DsbB structure, derived from the joint calculation with X-ray reflections and solid-state NMR restraints, into the lipid bilayer and performed MD simulations to provide a mechanistic view of DsbB function in the membrane. Further, we revealed the membrane topology of DsbB by selective proton spin diffusion experiments, which directly probe the correlations of DsbB with water and lipid acyl chains. NMR data also support the model of a flexible periplasmic loop and an interhelical hydrogen bond between Glu26 and Tyr153.

Original languageEnglish (US)
Pages (from-to)1670-1682
Number of pages13
JournalJournal of Molecular Biology
Issue number10
StatePublished - May 27 2013


  • DsbB
  • disulfide bond generation
  • membrane protein
  • molecular dynamics simulation
  • solid-state NMR

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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