Figure 4 | Scientific Reports

Figure 4

From: First crystal structures of 1-deoxy-d-xylulose 5-phosphate synthase (DXPS) from Mycobacterium tuberculosis indicate a distinct mechanism of intermediate stabilization

Figure 4

Comparison of drDXPS and MtDXPS enamine intermediate active sites. (a) Ser-network/H-bonds stabilizing the enamine intermediate. Residues from MtDXPS are colored in cyan, while the corresponding residues from drDXPS (PDB ID: 6OUW) are colored in yellow. Hydrogen bonds are shown as dashed lines with distances in Ångström. (b) “Fork” motif. The “fork”-like motif found in the intermediate structure is highlighted in cyan, the similar motif in drDXS is colored in yellow. The key difference is the presence of Glu293 in the MtDXPS structure. (c) ESSH sequence motif. The ESSH sequence motif found in the ∆MtDXPS structures is shown in pink. The table shows the sequence alignment of bacterial DXPS, with several sequences bearing the ESSH sequence motif shown for representation, highlighted with a pink box.

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