journal menu
![[Figure 3]](dw5165fig3mag.jpg)
|
|
Figure 3
The position of the acyl chain varies in the Gcn5 active site. (a) Overall structure of the catalytic domain of hsGcn5L2, shown in cartoon representation, bound to propionyl-CoA (cyan). The catalytic site is outlined with a black rectangle, where the catalytic water molecule is shown as a blue sphere and the acyl-CoA is depicted in stick representation. Close-up views of the active site of hsGcn5L2 bound to (b) acetyl-CoA (green), (c) propionyl-CoA (cyan) or (d) butyryl-CoA (orange). (e) Structural alignment of the three acyl-CoA molecules in the Gcn5 active site. (f, g, h) Close-up views of the different acyl groups: (f) acetyl-CoA, (g) propionyl-CoA and (h) butyryl-CoA. (i, j) Torsion angles adopted by the (i) propionyl and (j) butyryl moieties. |
![[Figure 3]](dw5165fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
