 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 6]](hv5157fig6mag.jpg)
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Figure 6
Stereoview of predicted acetoacetate binding to porcine SCOT inferred from the binding position of the glycerol in our glycerol-binding subunit. The binding position we observed for the glycerol is shown by a glycerol molecule with C atoms coloured grey and O atoms coloured red; the predicted positions of the acetoacetate and the CoA thioester are shown with C atoms coloured green and O atoms coloured red. The C atoms of the SCOT residues that interact with the glycerol molecule in the SCOT–glycerol complex are shown in pink, with O and N atoms coloured red and blue, respectively. The secondary structure in the region is shown as a transparent cartoon with dynamic domain 1 coloured pink and dynamic domain 2 coloured cyan. The position of the glutamyl thioester was modelled on the YdiF–CoA intermediate with the glutamyl in conformation I (Rangarajan et al., 2005  ). In this position it would be too far away from the acetoacetate for nucleophilic attack and must move into conformation II (the same conformation as Glu305 in our glycerol-bound subunit) for the reaction to proceed. |
![[Figure 6]](hv5157fig6.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
