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H-1, C-13 and N-15 resonance assignments and peptide binding site chemical shift perturbation mapping for the Escherichia coli redox enzyme chaperone DmsD

TitleH-1, C-13 and N-15 resonance assignments and peptide binding site chemical shift perturbation mapping for the Escherichia coli redox enzyme chaperone DmsD
Publication TypeJournal Article
Year of Publication2013
AuthorsStevens, CM, Okon, M, McIntosh, LP, Paetzel, M
JournalBIOMOLECULAR NMR ASSIGNMENTS
Volume7
Pagination193-197
Date PublishedOCT
ISSN1874-2718
Abstract

Herein are reported the mainchain H-1, C-13 and N-15 chemical shift assignments and amide N-15 relaxation data for Escherichia coli DmsD, a 23.3 kDa protein responsible for the correct folding and translocation of the dimethyl sulfoxide reductase enzyme complex. In addition, the observed amide chemical shift perturbations resulting from complex formation with the reductase subunit DmsA leader peptide support a model in which the 44 residue peptide makes extensive contacts across the surface of the DmsD protein.

DOI10.1007/s12104-012-9408-8