Fig. 4: Structural model of monomer vAlaS (CB_2) (red) and overlay with bacterial AlaS (blue) from R. capsulatus using AlphaFold. | Nature Communications

Fig. 4: Structural model of monomer vAlaS (CB_2) (red) and overlay with bacterial AlaS (blue) from R. capsulatus using AlphaFold.

From: Identification of Shemin pathway genes for tetrapyrrole biosynthesis in bacteriophage sequences from aquatic environments

Fig. 4

The dimer structure of vAlaS is depicted transparently in conjunction with its second monomer. Yellow spheres represent the pyridoxal phosphate (PLP) cofactor, one on each monomer. Glycine binding site (green circle) and succinyl-CoA binding site (purple circle). The lower picture shows an enhanced view of the PLP binding site where a Schiff’s base is formed with amino acid residue K248 (R. capsulatus numbering). A PDB file of the vAlaS modeled structure is available as Supplementary Data 7.

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