Sandbox Reserved 1063: Difference between revisions
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=='''Zinc-Dependent Transcriptional Regulator AdcR'''== | =='''Zinc-Dependent Transcriptional Regulator AdcR'''== | ||
===Introduction=== | ===Introduction=== | ||
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[[Image:Image1.jpg | 300 px|left|thumb| Members of the MarR protein family conserve a number of features including a general triangular shape, a two fold pseudosymmetric homo dimer, and a wingled helix-turn-helix pattern. Proteins 3BPX, 2FBK, 3KP5, and 2PFB (members of the MarR family) are pictured above.]] | [[Image:Image1.jpg | 300 px|left|thumb| Members of the MarR protein family conserve a number of features including a general triangular shape, a two fold pseudosymmetric homo dimer, and a wingled helix-turn-helix pattern. Proteins 3BPX, 2FBK, 3KP5, and 2PFB (members of the MarR family) are pictured above.]] | ||
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. | 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. | ||
<StructureSection load='3TGN' size='350' side='right' caption='3TGN' scene=''> | |||
== '''Zn(II) Binding''' == | == '''Zn(II) Binding''' == | ||
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. | 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. | ||