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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.

SUBMITTER: Ray LC

PROVIDER: S-EPMC6202225 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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Membrane association of monotopic phosphoglycosyl transferase underpins function.

Ray Leah C LC Das Debasis D Entova Sonya S Lukose Vinita V Lynch Andrew J AJ Imperiali Barbara B Allen Karen N KN

Nature chemical biology 20180516 6

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-b ...[more]

PMID: 29769739

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