CEEPC/IPM/CMSC - Abstrakt prezentace
WrbA, an E. coli stress-response protein probed by ion mobility mass spectrometry
Alan Kádek 1,2 *, Julien Marcoux 3, Iryna Kishko 4,5, Zdeněk Kukačka 1,2, Petr Man 1,2, Carol V. Robinson 3, Petr Novák 1,2, Rüdiger Ettrich 4,5, Jannette Carey 6
- Institute of Microbiology, ASCR, Prague, CZECH REPUBLIC
- Department of Biochemistry, Faculty of Science, Charles University in Prague, CZECH REPUBLIC
- Department of Chemistry, University of Oxford, UNITED KINGDOM
- Institute of Nanobiology and Structural Biology, ASCR, Nove Hrady, CZECH REPUBLIC
- Faculty of Sciences, University of South Bohemia, Nove Hrady, CZECH REPUBLIC
- Chemistry Department, Princeton University, Princeton, New Jersey, UNITED STATES OF AMERICA
Abstrakt
Tryptophan repressor-binding protein A (WrbA), more correctly called FMN-dependent NAD(P)H:quinone oxidoreductase, is an E. coli protein interesting for its involvement in bacterial responses to oxidative stress. Its biologically functional assembly is an obligate homotetramer held together by non-covalent interactions. Although a 1.2 Å high-resolution structure of this tetramer has been solved by X-ray crystallography, the dynamics of the protein in solution still remain under investigation. Of particular interest is the process of tetramer formation, during which WrbA is supposed to form a monomer-dimer-tetramer dynamic equilibrium.
In the present study, we utilized native electrospray ionization coupled with ion mobility mass spectrometry to gently transfer the intact non-covalent WrbA complexes into the gas phase while preserving their structure and to analyze the oligomeric states and conformations of this protein under different solution conditions. The results have shown a high stabilizing effect of FMN cofactor on the tetrameric structure of WrbA complex as well as provided an insight into the mechanism of the tetramer formation.
* Korespondující autor: kadek@biomed.cas.cz
Poděkování:
This work was funded by Instruct, part of the European Strategy Forum on Research Infrastructures (ESFRI) and supported by national member subscriptions; Institutional Research Concept of the Institute of Microbiology RVO 61388971; European Regional Development Funds (CZ.1.07/2.3.00/20.0055, CZ.1.07/2.3.00/30.0003 and CZ.1.05/1.1.00/02.0109); Research Project of Charles University (UNCE 204025/2012) and by the Grant Agency of Charles University (800413).
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