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. 2003 May 15;22(10):2334–2347. doi: 10.1093/emboj/cdg244

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graphic file with name cdg244f7a.jpg — Fig. 7. PCCβ homology model. (A) Structure-based sequence alignment of 12S and human PCCβ. Conserved residues are highlighted in black, and sites of PCCβ missense disease mutations are marked with an asterisk (*). The aligned CoA-binding motifs are boxed. (B) Electrostatic surface of the PCCβ homology modeled trimer, for the face involved in 12S inter-trimer packing (left) and for the solvent-exposed surface (right). (C) The PCCβ Arg165Gln, Arg165Trp and Glu168Lys missense mutations. Some or all of the interactions between Arg165 and Glu168, Asp105 would not be possible with Gln165 (cyan), Trp165 (purple) and Lys168 (green). (D) The PCCβ Arg410Trp missense mutation. Interactions with Ser254 in the opposing trimer would not be possible with Trp410 (purple). (E) The PCCβ Thr428Ile missense mutation. The hydrogen bond with Ser443 would not occur with Ile428 (magenta).

graphic file with name cdg244f7b.jpg — Fig. 7. PCCβ homology model. (A) Structure-based sequence alignment of 12S and human PCCβ. Conserved residues are highlighted in black, and sites of PCCβ missense disease mutations are marked with an asterisk (*). The aligned CoA-binding motifs are boxed. (B) Electrostatic surface of the PCCβ homology modeled trimer, for the face involved in 12S inter-trimer packing (left) and for the solvent-exposed surface (right). (C) The PCCβ Arg165Gln, Arg165Trp and Glu168Lys missense mutations. Some or all of the interactions between Arg165 and Glu168, Asp105 would not be possible with Gln165 (cyan), Trp165 (purple) and Lys168 (green). (D) The PCCβ Arg410Trp missense mutation. Interactions with Ser254 in the opposing trimer would not be possible with Trp410 (purple). (E) The PCCβ Thr428Ile missense mutation. The hydrogen bond with Ser443 would not occur with Ile428 (magenta).