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Team:HKU-Hong Kong/Modelling
From 2011.igem.org
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|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;"|Modelling | |style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;"|Modelling | ||
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| - | |style="width:900px; font size: 1.5em;color:#CC0000;"| | + | |style="width:900px; font size: 1.5em;color:#CC0000;"|The tetracycline inducible Tet repressor-operator system |
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TetR regulates the most abundant resistance mechanism against the antibiotic tetracycline in gram-negative bacteria. It consists of 208 residues, being folded into a 10 α – helices. α1 – α3 forms the DNA-binding domain, within which α2 – α3 constitute the classical helix-turn-helix motifs. α5 – α10 forms the binding domain of the tetracycline – magnesium complex, [MgTc]+, α5, α8 and α10 are helices of the rigid scaffold, within which α8 and α10 form the central part of the regulatory domain with the dyad related α8’ and α10’. α4 acts as the hydrophobic center of the DNA binding domain, and links the DNA-binding domain to the regulatory domain.<br/> | TetR regulates the most abundant resistance mechanism against the antibiotic tetracycline in gram-negative bacteria. It consists of 208 residues, being folded into a 10 α – helices. α1 – α3 forms the DNA-binding domain, within which α2 – α3 constitute the classical helix-turn-helix motifs. α5 – α10 forms the binding domain of the tetracycline – magnesium complex, [MgTc]+, α5, α8 and α10 are helices of the rigid scaffold, within which α8 and α10 form the central part of the regulatory domain with the dyad related α8’ and α10’. α4 acts as the hydrophobic center of the DNA binding domain, and links the DNA-binding domain to the regulatory domain.<br/> | ||
Revision as of 10:59, 30 September 2011
| Modelling | ||
| The tetracycline inducible Tet repressor-operator system | ||
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TetR regulates the most abundant resistance mechanism against the antibiotic tetracycline in gram-negative bacteria. It consists of 208 residues, being folded into a 10 α – helices. α1 – α3 forms the DNA-binding domain, within which α2 – α3 constitute the classical helix-turn-helix motifs. α5 – α10 forms the binding domain of the tetracycline – magnesium complex, [MgTc]+, α5, α8 and α10 are helices of the rigid scaffold, within which α8 and α10 form the central part of the regulatory domain with the dyad related α8’ and α10’. α4 acts as the hydrophobic center of the DNA binding domain, and links the DNA-binding domain to the regulatory domain.
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