Download MendeleyConformational changes of the Tet repressor induced by tetracycline trapping.
Orth, P., Cordes, F., Schnappinger, D., Hillen, W., Saenger, W., Hinrichs, W.(1998) J Mol Biol 279: 439-447
- PubMed: 9642048
- DOI: https://doi.org/10.1006/jmbi.1998.1775
- Primary Citation of Related Structures:
1A6I - PubMed Abstract:
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.
Organizational Affiliation:
Institut für Kristallographie, Freie Universität Berlin, Germany.
