This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1a6i
From Proteopedia
|
TET REPRESSOR, CLASS D VARIANT
Overview
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 Structure
1A6I is a Single protein structure of sequence from Escherichia coli. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Dec 18 14:10:03 2007
