Skip to main content
. Author manuscript; available in PMC: 2018 Feb 14.
Published in final edited form as: Biochemistry. 2008 Sep 17;47(40):10685–10693. doi: 10.1021/bi801309q

Figure 2.

Figure 2

The structure of K186A GDP-perosamine synthase in complex with GDP-perosamine. (a) Electron density corresponding to the bound nucleotide-linked sugar. The map was calculated with coefficients of the form (Fo - Fc), where Fo was the native structure factor amplitude and Fc was the calculated structure factor amplitude. Atoms corresponding to the PLP cofactor and the GDP-perosamine ligand were excluded from the coordinate file. The map was contoured at 3σ. (b) Close-up view of the active site with bound GDP-perosamine. Amino acids lying with ~3.5 Å of the PLP/GDP-perosamine complex are shown. Those residues highlighted in slate correspond to Subunit 3 in the x-ray coordinate file, whereas those displayed in green belong to Subunit 4. Residue labels ending with an asterisk correspond to Subunit 4. The PLP/GDP-perosamine complex is depicted in gold bonds. Potential hydrogen bonds are indicated by the dashed lines.