Mechanistic Basis for Ribosomal Peptide Backbone Modifications.
Journal
ACS central science
ISSN: 2374-7943
Titre abrégé: ACS Cent Sci
Pays: United States
ID NLM: 101660035
Informations de publication
Date de publication:
22 May 2019
22 May 2019
Historique:
received:
08
02
2019
entrez:
30
5
2019
pubmed:
30
5
2019
medline:
30
5
2019
Statut:
ppublish
Résumé
YcaO enzymes are known to catalyze the ATP-dependent formation of azoline heterocycles, thioamides, and (macro)lactamidines on peptide substrates. These enzymes are found in multiple biosynthetic pathways, including those for several different classes of ribosomally synthesized and post-translationally modified peptides (RiPPs). However, there are major knowledge gaps in the mechanistic and structural underpinnings that govern each of the known YcaO-mediated modifications. Here, we present the first structure of any YcaO enzyme bound to its peptide substrate in the active site, specifically that from
Identifiants
pubmed: 31139720
doi: 10.1021/acscentsci.9b00124
pmc: PMC6535971
doi:
Types de publication
Journal Article
Langues
eng
Pagination
842-851Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM097142
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM131347
Pays : United States
Organisme : NCRR NIH HHS
ID : S10 RR027109
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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