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Figure 4.
Figure 4. Lowest-Energy DNA-Bound AbrBN^55 Model from
Semi-Flexible Docking and Comparison to Unbound AbrBN^53
(A) Two views of the lowest-energy HADDOCK structure from the
semi-flexible docking studies. Disulfide linkages are shown as
spheres in the image. Insets show a detailed look at the
positioning of the arginine residues involved in binding.
(B) Overlay of unbound AbrBN^53 (red) and the lowest HADDOCK
score model of AbrBN^55 bound to abrB8 (blue). One monomer is
highlighted for clarity.
(C) The degree of structural
variation between the unbound AbrBN^53 NMR structure and the
modeled AbrBN^55 bound to abrB8, colored from white (little
variation) to red (large variation), as calculated in the Cα
alignment by THESEUS plotted on the refined AbrBN^53 solution
structure. The unbound and bound AbrBN^53 dimer structures
overlay with a Cα rmsd of 2.84 Å. LP1 and LP2 (chain A)
and LP1′ and LP2′ (chain B) are noted. Proteins are oriented
as depicted in Figure 1 on structures most similar to the
average structure in the ensemble reported by THESEUS.
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