Conformational changes of the Tet repressor induced by tetracycline trapping
Conformational changes of the Tet repressor induced by tetracycline trapping
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DOI:
10.1006/jmbi.1998.1775
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发表时间:
1998-06-05
影响因子:
5.6
通讯作者:
Hinrichs, W
中科院分区:
文献类型:
--
作者:
Orth, P;Cordes, F;Hinrichs, W
The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 Angstrom 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. (C) 1998 Academic Press Limited.