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Membrane association of monotopic phosphoglycosyl transferase underpins function.
Ray, Leah C; Das, Debasis; Entova, Sonya; Lukose, Vinita; Lynch, Andrew J; Imperiali, Barbara; Allen, Karen N.
Afiliación
  • Ray LC; Program in Biomolecular Pharmacology, Boston University School of Medicine, Boston, MA, USA.
  • Das D; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
  • Entova S; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
  • Lukose V; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
  • Lynch AJ; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
  • Imperiali B; Department of Chemistry, Boston University, Boston, MA, USA.
  • Allen KN; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA. imper@mit.edu.
Nat Chem Biol ; 14(6): 538-541, 2018 06.
Article en En | MEDLINE | ID: mdl-29769739
ABSTRACT
Polyprenol phosphate phosphoglycosyl transferases (PGTs) catalyze the first membrane-committed step in assembly of essential glycoconjugates. Currently there is no structure-function information to describe how monotopic PGTs coordinate the reaction between membrane-embedded and soluble substrates. We describe the structure and mode of membrane association of PglC, a PGT from Campylobacter concisus. The structure reveals a unique architecture, provides mechanistic insight and identifies ligand-binding determinants for PglC and the monotopic PGT superfamily.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Fosfatos / Campylobacter / Membrana Celular / Glicosiltransferasas Tipo de estudio: Risk_factors_studies Idioma: En Revista: Nat Chem Biol Asunto de la revista: BIOLOGIA / QUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Imprimir
XML
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Buscar en Google

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Fosfatos / Campylobacter / Membrana Celular / Glicosiltransferasas Tipo de estudio: Risk_factors_studies Idioma: En Revista: Nat Chem Biol Asunto de la revista: BIOLOGIA / QUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos