Proteomics

Dataset Information

0

Intact Mass analysis of class III lanthipeptide PneA


ABSTRACT: Intact Mass analysis of PneA under various modification states

ORGANISM(S): Streptococcus Pneumoniae Pt8114

SUBMITTER: Min Luo  

PROVIDER: PXD050940 | iProX | Tue Aug 13 00:00:00 BST 2024

REPOSITORIES: iProX

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Publications

Mechanistic insights into lanthipeptide modification by a distinct subclass of LanKC enzyme that forms dimers.

Li Yifan Y   Shao Kai K   Li Zhaoxing Z   Zhu Kongfu K   Gan Bee Koon BK   Shi Jian J   Xiao Yibei Y   Luo Min M  

Nature communications 20240817 1


Naturally occurring lanthipeptides, peptides post-translationally modified by various enzymes, hold significant promise as antibiotics. Despite extensive biochemical and structural studies, the events preceding peptide modification remain poorly understood. Here, we identify a distinct subclass of lanthionine synthetase KC (LanKC) enzymes with distinct structural and functional characteristics. We show that PneKC, a member of this subclass, forms a dimer and possesses GTPase activity. Through th  ...[more]

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