Mapping the architecture of the initiating phosphoglycosyl transferase from
E. coli
S. enterica serovar typhi
biochemistry
chemical biology
electron microscopy
glycoconjugate biosynthesis
lipopolysaccharide
mass spectrometry
membrane protein
molecular biophysics
structural biology
styrene maleic acid copolymer
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
15 Feb 2024
15 Feb 2024
Historique:
medline:
15
2
2024
pubmed:
15
2
2024
entrez:
15
2
2024
Statut:
epublish
Résumé
Bacterial cell surface glycoconjugates are critical for cell survival and for interactions between bacteria and their hosts. Consequently, the pathways responsible for their biosynthesis have untapped potential as therapeutic targets. The localization of many glycoconjugate biosynthesis enzymes to the membrane represents a significant challenge for expressing, purifying, and characterizing these enzymes. Here, we leverage cutting-edge detergent-free methods to stabilize, purify, and structurally characterize WbaP, a phosphoglycosyl transferase (PGT) from the
Identifiants
pubmed: 38358918
doi: 10.7554/eLife.91125
pii: 91125
doi:
pii:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIH HHS
ID : GM-039334
Pays : United States
Organisme : NIH HHS
ID : GM-131627
Pays : United States
Organisme : NIH HHS
ID : GM-134576
Pays : United States
Informations de copyright
© 2023, Dodge et al.
Déclaration de conflit d'intérêts
GD, AA, YH, WL, RV, BI No competing interests declared