Sandbox Reserved 1063: Difference between revisions

The binding of zinc metals creates a hydrogen bond network within the protein that connects the metal binding sites and the [https://en.wikipedia.org/wiki/DNA-binding_domain DNA binding domain]. The <scene name='69/694230/Hydrogen_bonding_1/5'>hydrogen bond network</scene> (<scene name='69/694230/Hydrogen_bonding_2/5'>with measurements</scene>) (residues in stick structures, colored by atom type) is characteristic of the MarR family as a whole and connects the metal binding pockets to the α4 helix also known as the recognition helix. <scene name='69/694230/Recognition_helix/3'>Several residues</scene> in the recognition helix recognize a sequence of DNA that is unknown at the moment; however, scientists are aware that the hydrogen bond network acts as an allosteric activator for the protein to bind DNA. The hydrogen bond network connects the α2 and α4 helix via hydrogen bonding between specific residues. After zinc is bound, a glutamate (E24) residue from a random coil accepts a hydrogen bond from the carboxamide end of an asparagine (N38) residue from the α2 helix. Then, a glutamine (Q40) residue from α2 helix accepts a hydrogen bond from a serine (S74) residue from the α4 helix <ref name="guerra" />. The binding of zinc allows for these conformational changes that induces the binding of DNA in order to activate genes.