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. 2021 Mar 16;12:1696. doi: 10.1038/s41467-021-21848-3

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© The Author(s) 2021, corrected publication 2021

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Fig. 6 — a Model for the CysB-mediated shuttling process. l-asparagine is activated by CysH and modified by CysJ, the AMDH domain, and CysQ as shown in Fig. 5. β-methoxy-l-isoasparagine is transferred from CysH to module 3 of CysK (M3) by CysB (green sphere). Condensation of the linker moiety with the pNBA₁-pABA₂ dipeptide leads to the formation of the shown tripeptide. b Deconvoluted protein MS analysis of CysB control; CysB incubated with free l-asparagine does not result in CysB loading; CysB incubated with l-asparagine and CysH leads to pH-sensitive loading of CysB (+114 m/z shift). c Protein MS analysis verifies the transfer of l-asparagine from CysB to CysK (M3) in the presence of CysH. Blue sphere: adenylation domain; gray sphere: thiolation domain; orange sphere: AMDH domain; red cross: inactive domain.