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1qpi
From Proteopedia
Revision as of 16:34, 29 September 2014 by OCA (Talk | contribs)
1qpi is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
