Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 425, Issue 10, Pages 1670-1682Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2013.02.009
Keywords
disulfide bond generation; DsbB; membrane protein; solid-state NMR; molecular dynamics simulation
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Funding
- National Institutes of Health [R01GM075937, S10RR025037, R01HL103999, R01GM073770 ARRA, NRSA F32GM095344]
- Molecular Biophysics Training Grant [PHS 5 T32 GM008276]
- Ullyot Fellowship
- National Institutes of Health Intramural Research Program of CIT
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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. (C) 2013 Elsevier Ltd. All rights reserved.
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