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Title: Membrane association of monotopic phosphoglycosyl transferase underpins function

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.

Authors:
ORCiD logo [1]; ORCiD logo [2];  [2]; ORCiD logo [2];  [3];  [2]; ORCiD logo [4]
  1. Boston Univ. School of Medicine, MA (United States)
  2. Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
  3. Boston Univ., MA (United States)
  4. Boston Univ. School of Medicine, MA (United States); Boston Univ., MA (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Inst. of Health
OSTI Identifier:
1438886
Grant/Contract Number:  
R01-GM039334; T32-GM007287; T32-GM008541; P41 GM103403
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Nature Chemical Biology
Additional Journal Information:
Journal Volume: 14; Journal Issue: 6; Journal ID: ISSN 1552-4450
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Ray, Leah C., Das, Debasis, Entova, Sonya, Lukose, Vinita, Lynch, Andrew J., Imperiali, Barbara, and Allen, Karen N. Membrane association of monotopic phosphoglycosyl transferase underpins function. United States: N. p., 2018. Web. doi:10.1038/s41589-018-0054-z.
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. United States. doi:10.1038/s41589-018-0054-z.
Ray, Leah C., Das, Debasis, Entova, Sonya, Lukose, Vinita, Lynch, Andrew J., Imperiali, Barbara, and Allen, Karen N. Wed . "Membrane association of monotopic phosphoglycosyl transferase underpins function". United States. doi:10.1038/s41589-018-0054-z. https://www.osti.gov/servlets/purl/1438886.
@article{osti_1438886,
title = {Membrane association of monotopic phosphoglycosyl transferase underpins function},
author = {Ray, Leah C. and Das, Debasis and Entova, Sonya and Lukose, Vinita and Lynch, Andrew J. and Imperiali, Barbara and Allen, Karen N.},
abstractNote = {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.},
doi = {10.1038/s41589-018-0054-z},
journal = {Nature Chemical Biology},
issn = {1552-4450},
number = 6,
volume = 14,
place = {United States},
year = {2018},
month = {5}
}

Journal Article:
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Cited by: 7 works
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