Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
Published version
Peer-reviewed
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Type
Article
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Authors
Moretto, L
Vance, S
Heames, B
Broadhurst, RW
Abstract
Interaction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5’-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation.
Description
Keywords
Acyl Carrier Protein, Alcohol Oxidoreductases, Bacterial Proteins, Binding Sites, Protein Conformation, Protein Structure, Tertiary, Substrate Specificity
Journal Title
Chemical Communications
Conference Name
Journal ISSN
1359-7345
1364-548X
1364-548X
Volume Title
53
Publisher
Royal Society of Chemistry
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Sponsorship
Wellcome Trust (094252/Z/10/Z)
The authors would like to thank the Wellcome Trust (grant number 094252/Z/10/Z) for funding this research. LM was supported by an EPSRC PhD studentship.