Subdomain dynamics enable chemical chain reactions in non-ribosomal peptide synthetases

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Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility

Subdomain Dynamics Enable Chemical Chain Reactions in Nonribosomal Peptide Synthetases

Subdomain Dynamics Enable Chemical Chain Reactions in Nonribosomal Peptide Synthetases

Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis

Subdomain dynamics enable chemical chain reactions in non-ribosomal peptide synthetases

Structural Biology of Nonribosomal Peptide Synthetases

Team:Heidelberg/NRPS

The inherent flexibility of type I non-ribosomal peptide synthetase multienzymes drives their catalytic activities

Subdomain dynamics enable chemical chain reactions in non-ribosomal peptide synthetases

Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis

Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity. - Abstract - Europe PMC

Computer-aided re-engineering of nonribosomal peptide and polyketide biosynthetic assembly lines - Natural Product Reports (RSC Publishing) DOI:10.1039/C9NP00021F

October 2014 – Wu Group