2020
DOI: 10.1101/2020.09.01.277863
|View full text |Cite
Preprint
|
Sign up to set email alerts
|

Exploring the conformational landscape of a lanthipeptide synthetase using native mass spectrometry

Abstract: Lanthipeptides are ribosomally-synthesized and post-translationally modified peptide (RiPP) natural products that are biosynthesized in a multistep maturation process by enzymes (lanthipeptide synthetases) that possess relaxed substrate specificity. Recent evidence has suggested that some lanthipeptide synthetases are structurally dynamic enzymes that are allosterically activated by precursor peptide binding, and that conformational sampling of the enzyme-peptide complex may play an important role in defining … Show more

Help me understand this report
View published versions

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

0
0
0

Publication Types

Select...

Relationship

0
0

Authors

Journals

citations
Cited by 0 publications
references
References 50 publications
0
0
0
Order By: Relevance

No citations

Set email alert for when this publication receives citations?