ArticleBiochemical and biophysical research communications2013
Chemical crosslinking and LC/MS analysis to determine protein domain orientation: application to AbrB.
Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis.Journal of molecular biology · 2020Article
- The Structure of the Biofilm-controlling Response Regulator BfmR from Acinetobacter baumannii Reveals Details of Its DNA-binding Mechanism.Journal of molecular biology · 2018Article
- Re-sensitizing Multidrug Resistant Bacteria to Antibiotics by Targeting Bacterial Response Regulators: Characterization and Comparison of Interactions between 2-Aminoimidazoles and the Response Regulators BfmR fromFrontiers in molecular biosciences · 2018Article
- Structure and DNA-binding traits of the transition state regulator AbrB.Structure (London, England : 1993) · 2014Article
- Cross-linking electrochemical mass spectrometry for probing protein three-dimensional structures.Analytical chemistry · 2014Article
- A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA.Journal of molecular biology · 2014Article
- Substitutional analysis of the C-terminal domain of AbrB revealed its essential role in DNA-binding activity.PloS one · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
To fully understand the modes of action of multi-protein complexes, it is essential to determine their overall global architecture and the specific relationships between domains and subunits. The transcription factor AbrB is a functional homotetramer consisting of two domains per monomer. Obtaining the high-resolution structure of tetrameric AbrB has been extremely challenging due to the independent character of these domains. To facilitate the structure determination process, we solved the NMR structures of both domains independently and utilized gas-phase cleavable chemical crosslinking and LC/MS(n) analysis to correctly position the domains within the full tetrameric AbrB protein structure.
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