Related Experiment Video
Updated: May 16, 2026

Application of an In vitro DNA Protection Assay to Visualize Stress Mediation Properties of the Dps Protein
Published on: May 31, 2013
Iron Binding Site in a Global Regulator in Bacteria - Ferric Uptake Regulator (Fur) Protein: Structure, Mössbauer
1Department of Chemistry, Chemical Biology, and Biomedical Engineering, Stevens Institute of Technology, Castle Point on Hudson Hoboken, NJ 07030, Unites States.
Abstract:
Fur protein plays key roles in regulating numerous genes in bacteria and is essential for intracellular iron concentration regulation. However, atomic level pictures of the iron binding site and its functional mechanism remain to be established. Here we present results of the first quantum chemical investigation of various first- and second-shell models and experimental Mössbauer data of E. Coli Fur, including 1) the first robust evidence that site 2 is the Fe binding site with a 3His/2Glu ligand set, being the first case in non-heme proteins, with computed Mössbauer data in excellent accord with experiment; 2) the first discovery of a conservative hydrogen bonding interaction in the iron binding site based on X-ray and homology structures; 3) the first atomic level hypothesis of active site reorganization upon iron concentration increase, triggering the conformational change needed for its function. These results shall facilitate structural and functional studies of Fur family proteins.
More Related Videos
Related Concept Videos
Transcriptional Regulation: Riboswitches
Microbes and Other Elemental Cycles
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Ligand Binding and Linkage
Cooperative Binding of Transcription Regulators
Global Regulatory Systems

