journal menu
![[Figure 5]](nz5020fig5mag.jpg)
|
|
Figure 5
(a) Superposition of the protomers of the monomeric and dimeric forms of EcoAcP. Pro79 is in the (b) cis (PDB entry 9sv2) and (c) trans (PDB entry 9sv1) conformations. Two hydrogen bonds between the backbone atoms of Glu78-Pro79 and those of residues Ile6-Ile7 in β1 are shown as green dashed lines. The trans conformation in the dimer allows interaction between the Glu78 and His80 side chains. (d, e) Fo − Fc omit maps contoured at 3σ of the (d) cis and (e) trans Glu78-Pro79 peptide. Residues 78–80 were omitted to generate the omit map. |
![[Figure 5]](nz5020fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
