Epitopes described in "Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer."

Reference
Article Authors:Ming Tang; Anna E Nesbitt; Lindsay J Sperling; Deborah A Berthold; Charles D Schwieters; Robert B Gennis; Chad M Rienstra
Article Title:Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer.
Reference Detail
Reference ID:1025555
Abstract: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.
Date:2013
Reference Type:Literature
PubMed ID:23416557
Journal:J Mol Biol
Journal Volume:425
Article Pages:1670-82
Journal ISSN:1089-8638
Article Chemical List:Bacterial Proteins;Disulfides;DsbB protein, Bacteria;Escherichia coli Proteins;Lipid Bilayers;Membrane Proteins
Article MeSH List:Amino Acid Sequence; Bacterial Proteins(biosynthesis; chemistry); Crystallography, X-Ray; Disulfides(chemistry; metabolism); Escherichia coli Proteins(biosynthesis; chemistry); Hydrogen Bonding; Lipid Bilayers(chemistry; metabolism); Membrane Proteins(biosynthesis; chemistry); Models, Molecular; Molecular Dynamics Simulation; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Substrate Specificity
Curation Last Updated:2014-10-03 22:51:56