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Membrane association of monotopic phosphoglycosyl transferase underpins function.

Nature chemical biology (2018-05-18)
Leah C Ray, Debasis Das, Sonya Entova, Vinita Lukose, Andrew J Lynch, Barbara Imperiali, Karen N Allen
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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Millipore
Cocktail di inibitori delle proteasi, set III, senza EDTA, Protease inhibitor cocktail III, EDTA-free for inhibiting aspartic, cysteine, and serine proteases as well as aminopeptidases in mammalian cells and tissues.