Figure 4
Structural differences between HinfPDH and its structural homologues. (a) Superimposition of HinfPDH, AaeoPDH, SthePDH and SyneADH reveals unique structural differences in HinfPDH including a missing α–β motif, a shorter Lβ5–β6 loop, and an extra C-terminal helix. HinfPDH is colored green or orange for each monomer. The AaeoPDH, SthePDH and SyneADH structures are colored magenta, yellow and blue, respectively. Bound tyrosine and NAD+ molecules are shown in ball-and-stick representation. (b) Enlarged view of the area around the α–β motif showing that HinfPDH is missing the α–β motif compared with AaeoPDH, SthePDH and SyneADH. (c) Enlarged view of the area around Lβ5–β6. Lys111 of HinfPDH is shown with a green backbone, Ser155 of AaeoPDH is in magenta and Gln120 of SyneADH is in blue. (d) Enlarged view of the C-terminal area showing that an extra C-terminal helix is present in HinfPDH. The α7 and α8 helices of HinfPDH superimposed onto structurally equivalent helices in AaeoPDH, SthePDH and SyneADH are also indicated. |