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Protein Science (2008), 17:199-204. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy

Ying Li1, Deborah A. Berthold2,3, Robert B. Gennis1,2,3, and Chad M. Rienstra1,2,3

1 Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA
2 Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA
3 Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA

(RECEIVED September 5, 2007; FINAL REVISION November 6, 2007; ACCEPTED November 10, 2007)

The Escherichia coli inner membrane enzyme DsbB catalyzes disulfide bond formation in periplasmic proteins, by transferring electrons to ubiquinone from DsbA, which in turn directly oxidizes cysteines in substrate proteins. We have previously shown that DsbB can be prepared in a state that gives highly resolved magic-angle spinning (MAS) NMR spectra. Here we report sequential 13C and 15N chemical shift assignments for the majority of the residues in the transmembrane helices, achieved by three-dimensional (3D) correlation experiments on a uniformly 13C, 15N-labeled sample at 750-MHz 1H frequency. We also present a four-dimensional (4D) correlation spectrum, which confirms assignments in some highly congested regions of the 3D spectra. Overall, our results show the potential to assign larger membrane proteins using 3D and 4D correlation experiments and form the basis of further structural and dynamical studies of DsbB by MAS NMR.

Keywords: solid-state NMR; membrane protein; chemical shift assignment; magic-angle spinning; disulfide bond formation


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