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. Author manuscript; available in PMC: 2012 Sep 2.
Published in final edited form as: J Mol Biol. 2011 Jun 22;411(5):999–1016. doi: 10.1016/j.jmb.2011.06.032

Fig. 4. Comparison of the apo and DD2-bound KSHV Pr crystal structures.

Fig. 4

(a) The dimer interface of KSHV Pr (2PBK) consists of two helices from each monomeric unit (helix 5, tan, monomer A; light blue, monomer B), which stabilize the active site (cyan) via the C-terminal helix 6 and occlude the Trp109 (red). (b) The Met197 and Ile201 sidechains from helix 5 of monomer B (orange) form hydrophobic interactions with Trp109 of monomer A. Both Δ196-DD2 monomer A (c) and monomer B (Fig. S5) exhibit independent DD2 binding pockets in which the Trp109 sidechain indole ring (red) adopts an “open” form (d). See also Movie S2.