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The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA Complex

This version is not peer-reviewed.

Submitted:

09 November 2020

Posted:

10 November 2020

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Abstract
Ferric uptake regulation protein is a repressor protein which binds an AT rich region of DNA (the iron box). Fur binds as a dimer in a helix turn helix mode and it is activated by iron(II) and other divalent transition metal ions at elevated concentrations in a process to regulate the ion uptake. Each transition metal ion induces certain conformational changes to aid the Fur binding, both the N-terminal and C-terminal domains take part in binding to DNA in addition to His 88 and His 86 residues. The process is discussed in view of experimental reports. Fe(II), Mn(II) and Co(II) activate Fur to bind DNA experimentally but Zinc plays a structural role and does not activate Fur to bind DNA.
Keywords: 
Ferric Uptake Regulation; Fur, Iron(II), Molecular dynamics; DNA; protein
Subject: 
Biology and Life Sciences  -   Biochemistry and Molecular Biology
Copyright: This open access article is published under a Creative Commons CC BY 4.0 license, which permit the free download, distribution, and reuse, provided that the author and preprint are cited in any reuse.

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