Ontology highlight
ABSTRACT:
SUBMITTER: Eisenmann A
PROVIDER: S-EPMC2279313 | biostudies-literature | 2005 Aug
REPOSITORIES: biostudies-literature
Protein science : a publication of the Protein Society 20050629 8
The carboxy-terminal domain of the transcription factor Escherichia coli NusA, NusACTD, interacts with the protein N of bacteriophage lambda, lambdaN, and the carboxyl terminus of the E. coli RNA polymerase alpha subunit, alphaCTD. We solved the solution structure of the unbound NusACTD with high-resolution nuclear magnetic resonance (NMR). Additionally, we investigated the binding sites of lambdaN and alphaCTD on NusACTD using NMR titrations. The solution structure of NusACTD shows two structur ...[more]