2trt
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(New page: 200px<br /><applet load="2trt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2trt, resolution 2.5Å" /> '''TETRACYCLINE REPRESSO...)
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Revision as of 11:59, 21 November 2007
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TETRACYCLINE REPRESSOR CLASS D
Overview
The most frequently occurring resistance of Gram-negative bacteria against, tetracyclines is triggered by drug recognition of the Tet repressor. This, causes dissociation of the repressor-operator DNA complex and enables, expression of the resistance protein TetA, which is responsible for active, efflux of tetracycline. The 2.5 angstrom resolution crystal structure of, the homodimeric Tet repressor complexed with tetracycline-magnesium, reveals detailed drug recognition. The orientation of the operator-binding, helix-turn-helix motifs of the repressor is inverted in comparison with, other DNA binding proteins. The repressor-drug complex is unable to, interact with DNA because the separation of the DNA binding motifs is 5, angstroms wider than usually observed.
About this Structure
2TRT is a Single protein structure of sequence from Escherichia coli with MG and TAC as ligands. This structure superseeds the now removed PDB entry 1TRT. Full crystallographic information is available from OCA.
Reference
Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance., Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W, Science. 1994 Apr 15;264(5157):418-20. PMID:8153629
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