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Fig. 2 | BMC Microbiology

Fig. 2

From: Portability of the thiolation domain in recombinant pyoverdine non-ribosomal peptide synthetases

Fig. 2

T domain interactions that are affected by substitution of alternative domains into PvdD. a Domain architecture of PvdD with the first module shown in blue and the second module shown in red. (b-d) Alternative domains substituted into PvdD are depicted in green: (b) C-A domain substitution; (c) T-C-A domain substitution; or (d) T domain substitution. In each panel, non-cognate (i.e., potentially disrupted) interactions between T domains and other domains are labelled according to the following scheme: (i) when an A domain passes a substrate to a non-cognate T domain; (ii) when a T domain passes a substrate to a non-cognate upstream C domain; or (iii) when a T domain passes a substrate to a non-cognate downstream C domain. The NRPS modules from which the C-A and T-C-A domains were sourced for substitution into PvdD are those labelled Ser1, Ser2 and fhOrn1 in Fig. 5

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