Quaternary Structure of the Tryptophan Synthase α-Subunit Homolog BX1 from Zea mays
2019
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.
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