Structure-Function Analysis of the S-Glycosylation Reaction in the Biosynthesis of Lincosamide Antibiotics.
Biosynthesis
Glycosyltransferase
Lincosamides
Natural product
X-ray Crystallography
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
17 07 2023
17 07 2023
Historique:
received:
08
04
2023
medline:
12
7
2023
pubmed:
24
5
2023
entrez:
24
5
2023
Statut:
ppublish
Résumé
The S-glycosyltransferase LmbT, involved in the biosynthesis of lincomycin A, is the only known enzyme that catalyzes the enzymatic incorporation of rare amino acid L-ergothioneine (EGT) into secondary metabolites. Here, we show the structure and function analyses of LmbT. Our in vitro analysis of LmbT revealed that the enzyme shows promiscuous substrate specificity toward nitrogenous base moieties in the generation of unnatural nucleotide diphosphate (NDP)-D-α-D-lincosamides. Furthermore, the X-ray crystal structures of LmbT in its apo form and in complex with substrates indicated that the large conformational changes of the active site occur upon binding of the substrates, and that EGT is strictly recognized by salt-bridge and cation-π interactions with Arg260 and Trp101, respectively. The structure of LmbT in complex with its substrates, the docking model with the EGT-S-conjugated lincosamide, and the structure-based site-directed mutagenesis analysis revealed the structural details of the LmbT-catalyzed S
Identifiants
pubmed: 37222528
doi: 10.1002/anie.202304989
doi:
Substances chimiques
Anti-Bacterial Agents
0
Lincosamides
0
Lincomycin
BOD072YW0F
Glycosyltransferases
EC 2.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202304989Informations de copyright
© 2023 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.
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