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

Olson, Andrew L

Bobay, Benjamin G

Melander, Christian

Cavanagh, John

2023-09-01T14:04:23Z

2023-09-01T14:04:23Z

2012-04

2023-09-01T14:04:22Z

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 backbone and sidechain resonance assignments and secondary structure prediction for the full-length AbrB protein from B. anthracis.

1874-2718

1874-270X

https://hdl.handle.net/10161/28897

eng

Springer Science and Business Media LLC

Biomolecular NMR assignments

10.1007/s12104-011-9333-2

Bacillus anthracis

Bacterial Proteins

DNA-Binding Proteins

Transcription Factors

Nuclear Magnetic Resonance, Biomolecular

Protein Structure, Secondary

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

Journal article

Bobay, Benjamin G|0000-0003-4775-3686

95

98

1

Duke

School of Medicine

Clinical Science Departments

Radiology

Published

6