Volume 17, Issue 2, Pages 202-210 (February 2009) Structural Basis for p300 Taz2-p53 TAD1 Binding and Modulation by Phosphorylation  Hanqiao Feng, Lisa M. Miller Jenkins, Stewart R. Durell, Ryo Hayashi, Sharlyn J. Mazur, Scott Cherry, Joseph E. Tropea, Maria Miller, Alexander Wlodawer, Ettore Appella, Yawen Bai  Structure  Volume 17, Issue 2, Pages 202-210 (February 2009) DOI: 10.1016/j.str.2008.12.009 Copyright © 2009 Elsevier Ltd Terms and Conditions

Figure 1 Structure of the Taz2-p532–39 Complex (A) Stereo image of the overlay of ten lowest-energy NMR structures of the complex between p5315–27 (magenta) and the Taz2 domain of p300 (gray). The structures are superimposed on the Cα traces. (B) Plot of backbone amide 15N-{1H} heteronuclear NOEs of p532–39. (C) Cylinder model of the average conformation of the complex. p53 is shown in magenta and the helices of Taz2 are shown in blue (α1), lilac (α2), orange (α3), and red (α4). Zinc ions in Taz2, modeled as green spheres, were added according to zinc-coordination distances into the known binding cage. (D) Secondary chemical shift difference of p532-39 in the complex (measured Cα chemical shift − random coil value). Structure 2009 17, 202-210DOI: (10.1016/j.str.2008.12.009) Copyright © 2009 Elsevier Ltd Terms and Conditions

Figure 2 Stabilizing Interactions between p532–39 and Taz2 (A) Model of the Taz2-p532–39 complex, showing residues that make hydrophobic contacts. Contacting residues are labeled in white for Taz2 (gray surface representation) and red for p532–39 (blue ribbon). (B) Model of the Taz2-p532–39 complex, colored by electrostatic potential (red represents negative, blue indicates positive). Taz2 is shown in a solid representation, and p532–39 as a mesh. (C) Model of the Taz2-p532–39 complex, showing residues that make electrostatic contacts. Contacting residues are labeled in white for Taz2 (gray surface representation) and red for p532–39 (blue ribbon). Structure 2009 17, 202-210DOI: (10.1016/j.str.2008.12.009) Copyright © 2009 Elsevier Ltd Terms and Conditions

Figure 3 Effect of p53 Phosphorylation on Taz2 Conformation (A) Overlay of a selected region of 2D 1H-15N HSQC spectra of 15N-labeled Taz2 complexed with p532–39 (black) and in complex with p531–39Thr18p (red). (B) Model of Taz2-p532–39 complex showing residues with significant changes in their amide chemical shifts upon addition of p531–39Thr18p. Residues of Taz2 (space-fill) with chemical shift changes shown in magenta; the two nearby arginine residues of Taz2 are shown in purple. The side chain of Thr18 of p53 (blue ribbon) is shown as sticks. Structure 2009 17, 202-210DOI: (10.1016/j.str.2008.12.009) Copyright © 2009 Elsevier Ltd Terms and Conditions