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Exploring the selectivity and engineering potential of an NRPS condensation domain involved in the biosynthesis of the thermophilic siderophore fuscachelin

ABSTRACT: Condensation (C) domains are the key component linking different monomers together, typically forming peptide bonds and occasionally ester bonds, during the nonribosomal peptide synthetase (NRPS). While A domains have been well characterised due to their role in selectivity of the monomers and functioning as a gate keeper in the NRPS biosynthesis, C domains have been a subject of debate as they have not demonstrated signs of “A-domain like” side chain selectivity of its acceptor side. Here, we report our biochemical and structural characterisation of the selectivity of the fuscachelin C3-domain showing that it is not broadly flexible for monomers at the acceptor site, suggesting the need to consider C-domain mutation regarding future NRPS engineering.

INSTRUMENT(S): Bruker Daltonics micrOTOF series, Orbitrap Fusion, Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Joel Steele

LAB HEAD: Max Cryle

PROVIDER: PXD040334 | Pride | 2023-06-02

REPOSITORIES: Pride

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			Action	DRS
	F1RS20210312_MC_TO_WT_BA3_Leu_E1.raw	Raw
	F1RS20210312_MC_TO_WT_BA3_Leu_E2.raw	Raw
	F1RS20210312_MC_TO_WT_BA3_Leu_E3.raw	Raw
	F1RS20210723_TO_GSRTAW_BA3_Gly_E1.raw	Raw
	F1RS20210723_TO_GSRTA_BA3_Gly_E1.raw	Raw

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