Sandbox Reserved 1063: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
<StructureSection load='3TGN' size='350' | <StructureSection load='3TGN' size='350' side='right' caption='3TGN' scene='3TGN' /> | ||
| Line 16: | Line 16: | ||
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 <font color='blue'>alpha helix 1</font>, <font color='gold'>alpha helix 5</font>, and the <font color='orange'>alpha helix 6</font>. This domain is connected to the HTH winged domain with the long <font color='gold'>alpha helix 5</font>. This dimerization domain connects to the DNA binding domain and together with the <font color='blue'>alpha 1</font> <font color='turquoise'>alpha 2</font> 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. | 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 <font color='blue'>alpha helix 1</font>, <font color='gold'>alpha helix 5</font>, and the <font color='orange'>alpha helix 6</font>. This domain is connected to the HTH winged domain with the long <font color='gold'>alpha helix 5</font>. This dimerization domain connects to the DNA binding domain and together with the <font color='blue'>alpha 1</font> <font color='turquoise'>alpha 2</font> loop make up the <scene name='69/694230/Alpha_1_alpha_2/1'>metal binding sites</scene><ref>PMID:22085181</ref>. 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. | ||
=== Binding Site 1 === | === Binding Site 1 === | ||