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Quaternary Structure of the Tryptophan Synthase α-Subunit Homolog BX1 from Zea mays
preprintsubmitted 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 SciencesFind out more...
Email Address of Submitting Authornorris.email@example.com
InstitutionOhio State University
ORCID For Submitting Author0000-0002-0121-5922
Declaration of Conflict of Interestno conflict of interest
Read the published paper
in Journal of the American Society for Mass Spectrometry