Extended Data Fig. 8: Details of the GudB-GltAB interaction.
From: A counter-enzyme complex regulates glutamate metabolism in Bacillus subtilis
(a) Key interactions between GltA (ovals on orange line) and two GudB protomers (ovals on green/major interaction and yellow line/minor interaction); salt bridges are shown in red and hydrogen bonds in blue. The border of ovals are colored based on domain/structural feature to which the residue belongs. (b) Binding to GltA stabilizes many loops in the cofactor binding domain of GudB. Shown are a GltA-bound GudB protomer (left, chain A in 7MFM) and a free GudB protomer in the same structure (right, chain B) in the ‘putty’ representation as implemented in PyMol. The radius of the ribbon increases from low to high B-factor and the Cα B-factors are shown in dark blue (lowest B-factor, 54) to red (highest B-factor, 163). nding site is located about 45 Å and 75 Å from the regulatory loop of GltA.
