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Quaternary Structure of the Tryptophan Synthase α-Subunit Homolog BX1 from Zea mays

preprint
submitted on 19.09.2019 and posted on 24.09.2019 by Andrew Norris, Florian Busch, Michael Schupfner, Reinhard Sterner, Vicki Wysocki
The manuscript describes the use of chemical cross-linking/mass spectrometry and mutagenesis to investigate the dimeric interface of the tryptophan synthase α-subunit homolog, BX1. This work indicates that BX1 homodimerization might have served as a mechanism to exclude an interaction with the tryptophan synthase β-subunit, TrpB, at an early time in evolution, thereby eliminating cross-talk between primary and secondary metabolism. This work would be of interest to mass spectrometrists and structural biologist as it presents a workflow to determine the physiological protein-protein interactions within crystal structures using chemical cross-linking/mass spectrometry and mutagenesis as complementary structural biology techniques, thereby eliminating ambiguity and potential mis-assignments due to the presence of additional (artificial) protein contacts formed during the crystallization process.

Funding

Resource for Native Mass Spectrometry Guided Structural Biology

National Institute of General Medical Sciences

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History

Email Address of Submitting Author

norris.702@osu.edu

Institution

Ohio State University

Country

United States

ORCID For Submitting Author

0000-0002-0121-5922

Declaration of Conflict of Interest

no conflict of interest

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in Journal of the American Society for Mass Spectrometry

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