1a6i
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TET REPRESSOR, CLASS D VARIANT
OverviewOverview
The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like, binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+., Recognition and binding of the inducer unleashes conformational changes, leading to the induced state of TetR. In the first step, the C-terminal, turn of alpha-helix 6 unwinds, thereby altering the orientation of, alpha-helix 4. This different orientation of alpha-helix 4 is stabilized, by a series of hydrogen bonds mediated through a chain of eight water, molecules. The alpha-helix 4 connects the DNA-binding domain, (alpha-helices 1 to 3) to the rigid TetR core, and thus regulates gene, expression through its respective orientations.
About this StructureAbout this Structure
1A6I is a Single protein structure of sequence from Escherichia coli. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Conformational changes of the Tet repressor induced by tetracycline trapping., Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W, J Mol Biol. 1998 Jun 5;279(2):439-47. PMID:9642048
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