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![[Figure 5]](ag5010fig5mag.jpg)
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Figure 5
Active-site architectures of MdCHS2, MdBIS3 and HaBPS. (a) The internal cavities of MdCHS2 (blue), MdBIS3 (green) and HaBPS (brown) are displayed as surface representations. Residues lining the cavities are displayed; the catalytic triads of each protein are labeled with black asterisks. Red asterisks highlight residues in CHS that are known to affect benzoyl-CoA substrate specificity. The novel pockets of MdBIS3 and HaBPS are labeled with magenta arrows. Residues are colored according to element: oxygen, red; nitrogen, blue; sulfur, yellow. (b) Naringenin, the product of CHS activity with 4-coumaroyl-CoA as a substrate, is modeled into the cavities of MdCHS2, HaBPS and MdBIS3. Naringenin is displayed in ball-and-stick representation. Coordinates for naringenin were obtained from superpositioning of the CHS–naringenin complex (PDB entry 1cgk). C atoms of the naringenin ligand are colored black and all other elements are colored as described above. |
![[Figure 5]](ag5010fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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