Sandbox Reserved 1063: Difference between revisions

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OCA, Zach LaRoche, Paxton Schowe, Geoffrey C. Hoops, Alexi Zaniker, Shandeep Singh, Isaac C. Gluesenkamp

Revision as of 21:50, 4 December 2017 view source Geoffrey C. Hoops (talk \| contribs) 208 edits No edit summary ← Older edit		Revision as of 21:56, 4 December 2017 view source Geoffrey C. Hoops (talk \| contribs) 208 edits No edit summary Newer edit →
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	==='''Structural Overview'''===		==='''Structural Overview'''===
	One of the two functional domains of AdcR is the <scene name='69/694230/Dimerization_domain/3'> dimerization domain</scene>. This domain connects and stabilizes the two pseudosymmetric ~~dimers~~ and is composed of the <scene name='69/694230/Alpha_1/1'>α1 helix</scene>, the C-terminus of the <scene name='69/694230/Alpha_five/1'>α5 helix</scene> , and the <scene name='69/694230/Alpha_6/1'>α6 helix</scene>. This domain is connected to the [https://en.wikipedia.org/wiki/DNA-binding_domain DNA binding domain] by the long α5 helix. The DNA binding domain stabilizes the major and minor groove of DNA via the <scene name='69/694230/Whth_4/7'>winged helix-turn-helix (wHTH)</scene> motif. The binding of Zinc to the <scene name='69/694230/2_binding_sites/4'>Zinc binding pocket</scene> induces a conformational change that allows for a <scene name='69/694230/Hydrogen_bonding_1/4'>hydrogen bond network</scene> between 4 specific residues. This network connects multiple helices from the metal binding pockets and DNA binding domain, and is believed play a critical role in the allosteric activation of AdcR, allowing the protein to bind exposed bases along the major and minor grooves of the DNA ligand <ref name="guerra">PMID:22085181</ref>. Thus, the protein is able to perform its biological function by activating transcription after binding DNA.		One of the two functional domains of AdcR is the <scene name='69/694230/Dimerization_domain/3'> dimerization domain</scene>. This domain connects and stabilizes the two pseudosymmetric protomers and is composed of the <scene name='69/694230/Alpha_1/1'>α1 helix</scene>, the C-terminus of the <scene name='69/694230/Alpha_five/1'>α5 helix</scene> , and the <scene name='69/694230/Alpha_6/1'>α6 helix</scene>. This domain is connected to the [https://en.wikipedia.org/wiki/DNA-binding_domain DNA binding domain] by the long α5 helix. The DNA binding domain stabilizes the major and minor groove of DNA via the <scene name='69/694230/Whth_4/7'>winged helix-turn-helix (wHTH)</scene> motif. The binding of Zinc to the <scene name='69/694230/2_binding_sites/4'>Zinc binding pocket</scene> induces a conformational change that allows for a <scene name='69/694230/Hydrogen_bonding_1/4'>hydrogen bond network</scene> between 4 specific residues. This network connects multiple helices from the metal binding pockets and DNA binding domain, and is believed play a critical role in the allosteric activation of AdcR, allowing the protein to bind exposed bases along the major and minor grooves of the DNA ligand <ref name="guerra">PMID:22085181</ref>. Thus, the protein is able to perform its biological function by activating transcription after binding DNA.