journal menu
![[Figure 4]](jb5017fig4mag.jpg)
|
|
Figure 4
The substrate-binding site of YncD shares similarities in its amino-acid composition and positive charge with that of the ferric citrate transporter FecA. (a) An electrostatic surface representation of the substrate-binding pocket of FecA in complex with Fe-citrate. For clarity, the surface of the open conformation of FecA (PDB entry 1kmo) is shown, with the extracellular loops of FecA that undergo a significant conformational change upon Fe-citrate binding shown as a cartoon view (Ferguson et al., 2002  ). (b) A stereoview of the FecA substrate-binding pocket showing residues involved in the coordination of Fe-citrate that do not change conformation on Fe-citrate binding as blue sticks and residues that change conformation as yellow sticks. (c) The electrostatic surface of YncD showing the location of Fe-citrate when the structure of FecA in complex with this ligand is superimposed with YncD. (d) A stereoview of the YncD substrate-binding pocket with conserved residues shown as purple sticks and Fe-citrate superimposed as in (c). Ferric citrate is shown in a sphere and stick representation in all panels. |
![[Figure 4]](jb5017fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
