Fig. 1: Structure of XylE and proposed experiment design. | Nature Communications

Fig. 1: Structure of XylE and proposed experiment design.

From: Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter

Fig. 1

a Topological and 3D structure of XylE (PDB: 4GBY)17. Three charged residues of interest in the proton binding site (D27, R133 and E206) are shown with their intra-residue distances. b Twenty-eight combinations of eight different protein states of XylE WT and three mutants (D27N, E206Q and E206Q&D27N) in the presence or absence of a substrate (xylose) and four combinations of XylE WT and mutant D27N in the presence or absence of an inhibitor (glucose) were studied in this work. All structural representations were generated using PyMol. Mutated residues are indicated by a star. Tables reporting experimental details for each ΔHDX-MS experiment are available as Supplementary Data File 1.

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