• Journal Article

1H, 13C, and 15N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis

Citation

Olson, A. L., Bobay, B. G., Melander, C., & Cavanagh, J. (2012). 1H, 13C, and 15N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis. Biomolecular NMR Assignments, 6(1), 95-98. DOI: 10.1007/s12104-011-9333-2

Abstract

The AbrB protein is a transcription factor that regulates the expression of numerous essential genes during the cells transition phase state. AbrB from Bacillus anthracis is, nototriously, the principal protein responsible for anthrax toxin gene expression and is highly homologous to the much-studied AbrB protein from Bacillus subtilis having 85% sequence identity and the ability to regulate the same target promoters. Here we report back-bone and sidechain resonance assignments and secondary structure prediction for the full-length AbrB protein from B. anthracis.