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Sandbox GGC3
From Proteopedia
(Difference between revisions)
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The subunits of the protein consist of a central <scene name='75/752266/Winged_hth_monomer/1'>winged helix-turn-helix (residues 33-112)</scene>. A helix-strand-helix occupies <scene name='75/752266/Nterm_monomer/1'>the N-terminal (residues 1-27)</scene> and a helix-loop motif occupies the <scene name='75/752266/Cterm_monomer/1'>C-terminus (residues 116-132)</scene>. The terminal structures allow the subunit to form its quaternary structure, and the central winged HTH is the functional region of the protein. | The subunits of the protein consist of a central <scene name='75/752266/Winged_hth_monomer/1'>winged helix-turn-helix (residues 33-112)</scene>. A helix-strand-helix occupies <scene name='75/752266/Nterm_monomer/1'>the N-terminal (residues 1-27)</scene> and a helix-loop motif occupies the <scene name='75/752266/Cterm_monomer/1'>C-terminus (residues 116-132)</scene>. The terminal structures allow the subunit to form its quaternary structure, and the central winged HTH is the functional region of the protein. | ||
| - | The helicies of the protein insert into the major grooves of the DNA, with the wings inserting into the minor grooves. The wing is inserted by Gly101 at the tip, allowing a deeper insertion into the minor groove than otherwise possible. Leu102 and Asn 103 interact with bases as well. Lys 79, Glu80, and Thr83 assist in association with DNA via hydrogen bonding in the case of Lys79 and Glu80, and van der Waals forces in the case of Thr83. No major conformational change occurs upon binding, but rather the DNA is bent. The DNA iteron is typically centered about a extended AT tract. | + | The helicies of the protein <scene name='75/752266/Dnabinding/1'>insert into the major grooves of the DNA</scene>, with the wings <scene name='75/752266/Dnabindingzoom/1'>inserting into the minor grooves</scene>. The wing is inserted by Gly101 at the tip, allowing a deeper insertion into the minor groove than otherwise possible. Leu102 and Asn 103 interact with bases as well. <scene name='75/752266/Dnabindingregions/1'>Lys 79, Glu80, and Thr83</scene> assist in association with DNA via hydrogen bonding in the case of Lys79 and Glu80, and van der Waals forces in the case of Thr83. No major conformational change occurs upon binding, but rather the DNA is bent. The DNA iteron is typically centered about a extended AT tract. |
Revision as of 16:45, 22 April 2018
RepA Multidrug-Resistance Initiator
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