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. Author manuscript; available in PMC: 2015 Jun 1.
Published in final edited form as: Curr Opin Struct Biol. 2014 Nov 25;0:112–121. doi: 10.1016/j.sbi.2014.10.006

Figure 4.

Figure 4

(a) The structure of PatF [37] represented as Figure 2a. Although the structure is that of a prenyl transferase, the protein is inactive. In other biosynthetic pathways, homologs of PatF have been shown to be active [35 and 36]

(b) a mechanism for the epimerization at the carbon adjacent to a thiazoline. The, study of a chemically related compound has led to the suggestion that in the patellamide pathway this is a spontaneous reaction [40]. However, an enzyme catalyzed processes has not been formally ruled out nor has epimerization adjacent to a thiazole been excluded

(c) cartoon representation of the structure of the PatG C-terminal DUF [39] reveals it to be a dimer, linked by zinc atoms. One monomer is colored as Figure 2a, the second monomer has duller colors

(d) the oxidase domain of PatG is highly conserved in other patellamide-like biosynthetic pathways with PatG homologs. Clustal Omega sequence alignment of the N-terminal oxidase domains of cyanobactin proteins PatG (Prochloron didemini), ArtG (Arthrospira platensis), MicG (Microcystis aeruginosa NIES-298), LynG (Lyngbya sp. PCC 8106), CyaG (Cyanothece sp. PCC7822) and TriG (Trichodesmium erythraeum IMS101). Figure created using ALINE.