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![[Figure 4]](gm5120fig4mag.jpg)
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Figure 4
E. coli FDP-ΔRd D52K and S262Y molecular tunnels. (a) Transparent solvent-accessible surface of the E. coli FDP-ΔRd D52K tetramer, colored as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif){kind=small} , showing both tunnel pathways. The long pathway (LP) connects the external surface of the protein with the di-iron catalytic site. Kr atoms (Kr1–Kr3) localized in the LP are shown as blue spheres and the 2m|Fo| − D|Fc| electron-density map is contoured at 1.5σ (gray mesh). The short pathway (SP) is in the opposite direction to the long pathway, connecting the di-iron site with the interior of the tetramer. The Lys52 and Ser262 residues are located near the SP and are shown with C atoms in cyan and dark red, respectively. Residues lining the SP and LP are represented by sticks with C atoms in gray, O atoms in red and N atoms in blue. (b) Long and short pathways from E. coli FDP-ΔRd D52K and S262Y variants. The residues at position 52 (cyan) and 262 (dark red) are located near the SP. The LP and SP are shown as a blue and gray mesh, respectively. |
![[Figure 4]](gm5120fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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