Chemical Crosslinking and LC/MS Analysis to Determine Protein Domain Orientation: Application to AbrB

Overview

Journal Biochem Biophys Res Commun

Publisher Elsevier

Specialty Biochemistry

Date 2013 Jan 15

PMID 23313475

Citations 7

Authors

Andrew L Olson

Fan Liu

Ashley T Tucker

Michael B Goshe

John Cavanagh

Affiliations

Soon will be listed here.

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.

Citing Articles

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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 from and QseB from spp.

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The Structure of the Biofilm-controlling Response Regulator BfmR from Acinetobacter baumannii Reveals Details of Its DNA-binding Mechanism.

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Structure and DNA-binding traits of the transition state regulator AbrB.

Olson A, Tucker A, Bobay B, Soderblom E, Moseley M, Thompson R Structure. 2014; 22(11):1650-6.

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Cross-linking electrochemical mass spectrometry for probing protein three-dimensional structures.

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