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. Author manuscript; available in PMC: 2017 Dec 6.
Published in final edited form as: Structure. 2016 Nov 3;24(12):2067–2079. doi: 10.1016/j.str.2016.09.012

Figure 4. Central β-strand Pivoting in the W196A Mutant Creates a Hydrophobic Border near the Dimerization Interface.

Figure 4

(A) Overlay of monomeric wild-type AIF (gray, PDB: 4BV6) and AIF78 W196A (color) highlights rotation of AIF’s central β-strand and capping β-hairpin at the FAD/C-domain interface.

(B) The Cβ-clasp region highlighting displacement of the clasp β-hairpin and the central β-strand.

(C) The H454-S480 hydrogen-bonding network (dashed line) in monomeric wild-type AIF (left) that is reorganized into S480-H457-Y476 in dimeric W196A (right). Oxygen, red; nitrogen, blue.

(D) The D444-R450 hydrogen bonding network (dashed line) in monomeric wild-type AIF (left) that is reorganized to include Q479 in dimeric W196A (right).

(E) The W477/I445/Y443 border (left) in monomeric wild-type AIF (top right) aligns to form a contiguous hydrophobic surface against the polar center of the dimer interface in dimeric W196A (bottom right).