Fig. 4 | Signal Transduction and Targeted Therapy

Fig. 4

From: Structural basis for the acetylation of histone H3K9 and H3K27 mediated by the histone chaperone Vps75 in Pneumocystis carinii

Fig. 4

Interfaces within the PcVps75 tetramer. a Loop 1 and loop 2 in protomer D are colored green. Loop 1 and loop 2 in protomer A are colored orange. Loop 1 and loop 2 in protomer B are colored green. I: Detailed view of the hydrophobic interface between LP1A and LP2D. The key interacting residues in LP1A and LP2D are colored orange and green, respectively. II: The salt bonds between LP2A and LP1D are shown as dotted lines. The key interacting residues in LP2A and LP1D are indicated in orange and green, respectively. III: The electrovalent bonds between calcium and LP2A and LP2D are shown as dotted lines. The key interacting residues in LP2A and LP2D are indicated in orange and green, respectively. “Ca” represents calcium ions. b The second, minor interface between protomers B and C is circled with a dotted line. Protomer B is colored orange, and protomer C is colored green

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