Journal: RSC Chemical Biology
Article Title: Natural Trojan horse inhibitors of aminoacyl-tRNA synthetases
doi: 10.1039/d0cb00208a
Figure Lengend Snippet: (A) Structures of albomycins, albomycin toxic moiety (SB-217452) and seryl-adenylate. (B) A scheme showing the biosynthesis, transport and intracellular processing of albomycin. IM – inner membrane, OM – outer membrane, BGC – biosynthetic gene cluster, SerRS – seryl-tRNA-synthetase. (C) The crystal structure of the FhuA outer membrane transporter in complex with albomycin (PDB ID: 1QKC ). Two conformational isomers of albomycin are shown (black arrows: 1 – extended form, 2 – compact form). A close-up view of the extended albomycin form binding site is shown, residues involved in the binding are indicated, hydrogen bonds are shown as black dashed lines. (D) The crystal structure of the FhuD periplasmic binding protein in complex with albomycin (PDB ID: 1K7S ). Residues involved in the formation of the albomycin binding site are indicated; hydrogen bonds are shown as black dashed lines. Electron density for the toxic moiety of albomycin is not observed in this structure.
Article Snippet: Presumably, Streptomyces sp. C and S. vitaminophilus ATCC 31673 produce different SB-217452-like nucleosides, since the ctj cluster lacks one of the rSAM enzymes, an ortholog of AbmJ, which is responsible for D-ribo to D-xylo epimerization of the furanose ring in albomycin.
Techniques: Binding Assay