Substrate recognition and ATPase activity of the E. coli cysteine/cystine ABC transporter YecSC-FliY.

ABSTRACT: Sulfur is essential for biological processes such as amino acid biogenesis, iron-sulfur cluster formation, and redox homeostasis. To acquire sulfur-containing compounds from the environment, bacteria have evolved high-affinity uptake systems, predominant among which is the ABC transporter family. Theses membrane-embedded enzymes use the energy of ATP hydrolysis for transmembrane transport of a wide range of biomolecules against concentration gradients. Three distinct bacterial ABC import systems of sulfur-containing compounds have been identified, but the molecular details of their transport mechanism remain poorly characterized. Here we provide results from a biochemical analysis of the purified Escherichia coli YecSC-FliY cysteine/cystine import system. We found that the substrate

SUBMITTER: Sabrialabed S 

PROVIDER: S-EPMC7170509 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature