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. 2012 Oct 26;287(50):41569–41575. doi: 10.1074/jbc.C112.421222

FIGURE 4.

FIGURE 4.

The TAT N terminus is essential and structurally plastic. A, ribbon representation of the D117A TAT crystal structure bound to Ac-CoA colored as in Fig. 2A. B, superposition of wild-type and D117A TAT structures. Green (protomer A) and magenta (protomer B), wild-type TAT crystallographic dimer; yellow (protomer A) and blue (protomer B), D117 A TAT dimer. Swapped elements are labeled in blue. *, pivot point. C, D117A TAT is a dimer in solution. Sedimentation coefficient distributions c(s) at 20 (orange) and 40 μm (red) are shown. D, mutants at the α1/central β-sheet interface result in higher-order oligomers as assayed by size-exclusion chromatography. Void volume, 17 min. E, normalized tubulin acetylation activity of TAT mutants color-coded to match the traces in D. Error bars indicate S.E. (n ≥ 3). Inset: normalized tubulin acetylation activity of 0/100, 25/75, 50/50, and 100/0% wild-type/D117A TAT mixtures.