1du7
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(New page: 200px<br /><applet load="1du7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1du7, resolution 2.51Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 11:28, 20 November 2007
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CRYSTAL STRUCTURE OF TET REPRESSOR CLASS D WITH 4-EPI-TETRACYCLINE
Overview
The tetracycline repressor (TetR) regulates the most abundant resistance, mechanism against the antibiotic tetracycline in grain-negative bacteria., The TetR protein and its mutants are commonly used as control elements to, regulate gene expression in higher eukaryotes. We present the crystal, structure of the TetR homodimer in complex with its palindromic DNA, operator at 2.5 A resolution. Comparison to the structure of TetR in, complex with the inducer tetracycline-Mg2+ allows the mechanism of, induction to be deduced. Inducer binding in the repressor core initiates, conformational changes starting with C-terminal unwinding and shifting of, the short helix a6 in each monomer. This forces a pendulum-like motion of, helix a4, which increases the separation of the attached DNA binding, domains by 3 A, abolishing the affinity of TetR for its operator DNA.
About this Structure
1DU7 is a Single protein structure of sequence from Escherichia coli with CTC as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system., Orth P, Schnappinger D, Hillen W, Saenger W, Hinrichs W, Nat Struct Biol. 2000 Mar;7(3):215-9. PMID:10700280
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