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Updated: May 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Chemical shift assignments and secondary structure prediction of the phosphorelay protein VanU from Vibrio
Benjamin G Bobay1, Richele J Thompson, Debra L Milton
1Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC, 27695, USA.
Abstract:
Vibrio anguillarum is a biofilm forming Gram-negative bacterium that survives prolonged periods in seawater and causes vibriosis in marine life. A quorum-sensing signal transduction pathway initiates biofilm formation in response to environmental stresses. The phosphotransferase protein VanU is the focal point of the quorum-sensing pathway and facilitates the regulation between independent phosphorelay systems that activate or repress biofilm formation. Here we report the (1)H, (13)C, and (15)N backbone and side chain resonance assignments and secondary structure prediction for VanU from V. anguillarum.
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