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

submitted on 19.09.2019, 15:47 and posted on 24.09.2019, 21:16 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.


Resource for Native Mass Spectrometry Guided Structural Biology

National Institute of General Medical Sciences

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Ohio State University


United States

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in Journal of the American Society for Mass Spectrometry