Mass spectrometry locates local and allosteric conformational changes that occur on cofactor binding

Rebecca Beveridge; Lukasz G. Migas; Karl A. P. Payne; Nigel S. Scrutton; David Leys; Perdita E. Barran

doi:10.1038/ncomms12163

Nature Communications (Jul 2016)

Mass spectrometry locates local and allosteric conformational changes that occur on cofactor binding

Rebecca Beveridge,
Lukasz G. Migas,
Karl A. P. Payne,
Nigel S. Scrutton,
David Leys,
Perdita E. Barran

Affiliations

Rebecca Beveridge: Michael Barber Centre for Collaborative Mass Spectrometry, School of Chemistry, Centre for Synthetic Biology of Fine and Speciality Chemicals, Manchester Institute of Biotechnology, University of Manchester
Lukasz G. Migas: Michael Barber Centre for Collaborative Mass Spectrometry, School of Chemistry, Centre for Synthetic Biology of Fine and Speciality Chemicals, Manchester Institute of Biotechnology, University of Manchester
Karl A. P. Payne: Michael Barber Centre for Collaborative Mass Spectrometry, School of Chemistry, Centre for Synthetic Biology of Fine and Speciality Chemicals, Manchester Institute of Biotechnology, University of Manchester
Nigel S. Scrutton: Michael Barber Centre for Collaborative Mass Spectrometry, School of Chemistry, Centre for Synthetic Biology of Fine and Speciality Chemicals, Manchester Institute of Biotechnology, University of Manchester
David Leys: Michael Barber Centre for Collaborative Mass Spectrometry, School of Chemistry, Centre for Synthetic Biology of Fine and Speciality Chemicals, Manchester Institute of Biotechnology, University of Manchester
Perdita E. Barran: Michael Barber Centre for Collaborative Mass Spectrometry, School of Chemistry, Centre for Synthetic Biology of Fine and Speciality Chemicals, Manchester Institute of Biotechnology, University of Manchester

DOI: https://doi.org/10.1038/ncomms12163
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 9

Abstract

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The decarboxylate enzyme Fdc1 requires a prenylated flavin mononucleotide co-factor for activity. Here, the authors use a variety of mass spectrometric techniques to observe the structural changes in this protein in response to co-factor binding.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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