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![[Figure 2]](gm5120fig2mag.jpg)
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Figure 2
Di-iron catalytic site of FDPs. (a) Representation of the Lys52 and Tyr262 residues from the di-iron second coordination sphere of E. coli FDP-ΔRd D52K/S262Y. Cartoon representation of the monomers, colored in dark red and cyan. (b) Representation of the Asp52 and Ser262 residues from the di-iron second coordination sphere of E. coli FDP (PDB entry 4d02). Cartoon representation of the monomers, colored in dark red and cyan. (c) Superposition of the di-iron second coordination spheres from E. coli FDP-ΔRd D52K (pink), S262Y (blue) and D52K/S262Y (green). (d) Superposition of the di-iron second coordination sphere from E. coli FDP-ΔRd D52K/S262Y (green) with G. intestinalis FDP (PDB entry 2q9u; orange). Fe atoms are represented as black spheres. The amino-acid residues and FMN are shown as sticks with C atoms in gray, N atoms in blue, O atoms in red and P atoms in orange. The μ-hydroxo bridge is shown as a red sphere. |
![[Figure 2]](gm5120fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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