-
Categories
-
Pharmaceutical Intermediates
-
Active Pharmaceutical Ingredients
-
Food Additives
- Industrial Coatings
- Agrochemicals
- Dyes and Pigments
- Surfactant
- Flavors and Fragrances
- Chemical Reagents
- Catalyst and Auxiliary
- Natural Products
- Inorganic Chemistry
-
Organic Chemistry
-
Biochemical Engineering
- Analytical Chemistry
- Cosmetic Ingredient
-
Pharmaceutical Intermediates
Promotion
ECHEMI Mall
Wholesale
Weekly Price
Exhibition
News
-
Trade Service
How do human immune molecules perceive and destroy disease-caused bacteria? Details of the molecular struggle between pathogenic bacteria and human immunity have been revealed by the University of East Anglia and the French Institute of Biological Structures, published in the journal Nature Communications.
university of East Anglia and the French Institute of Biological Structures (CEA-CNRSUGA) have now identified the structure of NsrR.
NsrR is a bacterial protein that binds to DNA and helps bacteria fight off nitric oxide released by humans at the beginning of an infection.
in order to resist the toxic nitric oxide on life, many bacteria gradually evolved to form a corresponding detection method.
most commonly used nitric oxide sensor for bacteria is the regulatory protein NsrR.
regulate proteins bound to DNA to control the turn on and off of specific genes.
NsrR contains a particular type of cofactor (an additional ingredient required for protein activity) called iron-sulfur clusters.
they are fragile, responsive and difficult to work together, recent work at the School of Chemistry and Biology at the University of East Anglia provides important new information about NsrR as a nitric oxide sensor.
team has identified the structure of the protein in two main forms, showing how NsrR responds to nitric oxide.
these structural changes show how NsrR switches between DNA-binding and unbound forms, enabling it to decide whether to produce enzymes that fight nitric oxide.
Professor Nick Le Brun, who led the effort, said: "NsrR belongs to a family of important but less well-understood regulators that aid bacteria in achieving a variety of important cellular functions.
many regulators have been proven or predicted to contain iron-sulfur clusters, but our work provides the first example of a fragile cluster binding structure that reveals a common mechanism for regulators to respond to different signals.
further, the structure also reveals that clusters and proteins work together in an unprecedented way.
the process by which pathogens survive the human immune response is complex, the more likely we are to develop intervention strategies to prevent such responses.
"