Membrane association of monotopic phosphoglycosyl transferase underpins function

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....

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Autores principales: Ray, Leah C., Das, Debasis, Entova, Sonya, Lukose, Vinita, Lynch, Andrew J., Imperiali, Barbara, Allen, Karen N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6202225/
https://www.ncbi.nlm.nih.gov/pubmed/29769739
http://dx.doi.org/10.1038/s41589-018-0054-z
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author Ray, Leah C.
Das, Debasis
Entova, Sonya
Lukose, Vinita
Lynch, Andrew J.
Imperiali, Barbara
Allen, Karen N.
author_facet Ray, Leah C.
Das, Debasis
Entova, Sonya
Lukose, Vinita
Lynch, Andrew J.
Imperiali, Barbara
Allen, Karen N.
author_sort Ray, Leah C.
collection PubMed
description 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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spelling pubmed-62022252018-11-16 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. Nat Chem Biol Article 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. 2018-05-16 2018-06 /pmc/articles/PMC6202225/ /pubmed/29769739 http://dx.doi.org/10.1038/s41589-018-0054-z Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Ray, Leah C.
Das, Debasis
Entova, Sonya
Lukose, Vinita
Lynch, Andrew J.
Imperiali, Barbara
Allen, Karen N.
Membrane association of monotopic phosphoglycosyl transferase underpins function
title Membrane association of monotopic phosphoglycosyl transferase underpins function
title_full Membrane association of monotopic phosphoglycosyl transferase underpins function
title_fullStr Membrane association of monotopic phosphoglycosyl transferase underpins function
title_full_unstemmed Membrane association of monotopic phosphoglycosyl transferase underpins function
title_short Membrane association of monotopic phosphoglycosyl transferase underpins function
title_sort membrane association of monotopic phosphoglycosyl transferase underpins function
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6202225/
https://www.ncbi.nlm.nih.gov/pubmed/29769739
http://dx.doi.org/10.1038/s41589-018-0054-z
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