Molecular characterization of the interaction of sialic acid with the periplasmic binding protein from Haemophilus ducreyi.

ABSTRACT: The primary role of bacterial periplasmic binding proteins is sequestration of essential metabolites present at a low concentration in the periplasm and making them available for active transporters that transfer these ligands into the bacterial cell. The periplasmic binding proteins (SiaPs) from the tripartite ATP-independent periplasmic (TRAP) transport system that transports mammalian host-derived sialic acids have been well studied from different pathogenic bacteria, including Haemophilus influenzae, Fusobacterium nucleatum, Pasteurella multocida, and Vibrio cholerae SiaPs bind the sialic acid N-acetylneuraminic acid (Neu5Ac) with nanomolar affinity by forming electrostatic and hydrogen-bonding interactions. Here, we report the crystal structure of a

SUBMITTER: Gangi Setty T 

PROVIDER: S-EPMC6311513 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature