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![[Figure 3]](ag5010fig3mag.jpg)
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Figure 3
Overall crystal structures of MdCHS2, MdBIS3 and HaBPS. (a) The asymmetric units of MdCHS2 (blue), MdBIS3 (green) and HaBPS (brown) contain the physiologically relevant homodimers. The polypeptide chains of each protein are represented as ribbons. The side chains of the active-site cysteines for each crystal structure are shown as sticks and labeled with asterisks. The N-terminus and C-terminus of the superposed structures are labeled N and C, respectively. The dashed box highlights the CoA tunnel and the displaced solvent loops near the CoA tunnels of BIS and BPS (see Fig. 4 ![[link]](../../../../../../logos/arrows/d_arr.gif) ). (b) The structure of BIS complexed with benzoyl-CoA. The surface of the protein dimer is displayed and each monomeric subunit is shown in ribbon representation with rainbow coloring from the N-terminus (blue) to the C-terminus (red). Benzoyl-CoA is displayed as spheres with atoms color-coded according to element: carbon, black; oxygen, red; phosphorus, orange; nitrogen, blue; sulfur, yellow. |
![[Figure 3]](ag5010fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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