Sandbox Reserved 1063: Difference between revisions

Consistent with AdcR's identity as a member of the MarR protein family, AdcR exhibits a triangular shape consisting of a two fold pseudosymetric homo dimer with its own unique winged helix-turn-helix [https://en.wikipedia.org/wiki/Helix-turn-helix (wHTH)] binding domain. This structure calls for multiple zinc binding sites that facilitate protein conformational change allowing for DNA binding and regulation through the wHTH domain.   

Zinc-Dependent Transcriptional Regulator AdcR has <scene name='69/694230/Two_binding_sites/1'>two binding sites</scene> on each of its two protomers and can bind a total of four Zn(II) per dimer. <scene name='69/694230/Dimerization_domain/1'>The dimerization domain</scene> is made up of the alpha 1 helix (blue), alpha 5 helix (yellow), and the alpha 6 helix (orange). This domain is connected to the HTH winged domain with the long alpha 5 helix (yellow). This dimerization domain connects to the DNA binding domain and together with the alpha 1 (blue) alpha 2 (light blue) loop make up the <scene name='69/694230/Alpha_1_alpha_2/1'>metal binding sites</scene>. Each protomer has one high affinity site (KZn1 = 10^12 M; pH 8) and one low affinity binding site (KZn2 = 10^7 M; pH 8). The metal binding pockets of the AdcR MarR transcriptional regulator are made up of the DNA binding domain with the extended alpha 1 and alpha 2 loop. The two different Zn(II) binding sites are connected via hydrogen bonding of the Nd1 atom of H108 and then liganding Oe1 atom of E41.