Open AccessMembrane association of monotopic phosphoglycosyl transferase underpins function
Author(s) -
Leah Ray,
Debasis Das,
Sonya Entova,
Vinita Lukose,
A.J. Lynch,
Barbara Imperiali,
Karen N. Allen
Publication year - 2018
Publication title -
nature chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.412
H-Index - 216
eISSN - 1552-4469
pISSN - 1552-4450
DOI - 10.1038/s41589-018-0054-z
Subject(s) - glycoconjugate , superfamily , transferase , biology , biochemistry , function (biology) , membrane protein , chemistry , membrane , computational biology , microbiology and biotechnology , enzyme , gene
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.