Structures of trehalose-6-phosphate synthase, Tps1, from the fungal pathogen
Cryptococcus
basidiomycetes
cryoelectron microscopy
fungal pathogens
trehalose
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
06 Aug 2024
06 Aug 2024
Historique:
medline:
31
7
2024
pubmed:
31
7
2024
entrez:
31
7
2024
Statut:
ppublish
Résumé
Invasive fungal diseases are a major threat to human health, resulting in more than 1.5 million annual deaths worldwide. The arsenal of antifungal therapeutics remains limited and is in dire need of drugs that target additional biosynthetic pathways that are absent from humans. One such pathway involves the biosynthesis of trehalose. Trehalose is a disaccharide that is required for pathogenic fungi to survive in their human hosts. In the first step of trehalose biosynthesis, trehalose-6-phosphate synthase (Tps1) converts UDP-glucose and glucose-6-phosphate to trehalose-6-phosphate. Here, we report the structures of full-length
Identifiants
pubmed: 39083421
doi: 10.1073/pnas.2314087121
doi:
Substances chimiques
trehalose-6-phosphate synthase
EC 2.4.1.15
Glucosyltransferases
EC 2.4.1.-
Antifungal Agents
0
Trehalose
B8WCK70T7I
Fungal Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2314087121Subventions
Organisme : HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID)
ID : 1P01AI104533
Organisme : HHS | NIH | NIAID | Division of Intramural Research (DIR, NIAID)
ID : T32AI052080
Déclaration de conflit d'intérêts
Competing interests statement:The authors declare no competing interest.