Substrate recognition and ATPase activity of the E. coli cysteine/cystine ABC transporter YecSC-FliY
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 295, Issue: 16, Page: 5245-5256
2020
- 11Citations
- 31Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations11
- Citation Indexes11
- 11
- CrossRef5
- Captures31
- Readers31
- 31
Article Description
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-binding protein FliY binds l -cystine, l -cysteine, and d -cysteine with micromolar affinities. However, binding of the l - and d -enantiomers induced different conformational changes of FliY, where the l - enantiomer–substrate-binding protein complex interacted more efficiently with the YecSC transporter. YecSC had low basal ATPase activity that was moderately stimulated by apo FliY, more strongly by d -cysteine–bound FliY, and maximally by l -cysteine– or l -cystine–bound FliY. However, at high FliY concentrations, YecSC reached maximal ATPase rates independent of the presence or nature of the substrate. These results suggest that FliY exists in a conformational equilibrium between an open, unliganded form that does not bind to the YecSC transporter and closed, unliganded and closed, liganded forms that bind this transporter with variable affinities but equally stimulate its ATPase activity. These findings differ from previous observations for similar ABC transporters, highlighting the extent of mechanistic diversity in this large protein family.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925817485474; http://dx.doi.org/10.1074/jbc.ra119.012063; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85083485627&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/32144203; https://linkinghub.elsevier.com/retrieve/pii/S0021925817485474; https://dx.doi.org/10.1074/jbc.ra119.012063
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know