Conformational changes of the Tet repressor induced by tetracycline trapping. Academic Article uri icon

Overview

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.

publication date

  • June 5, 1998

Research

keywords

  • Bacterial Proteins
  • Repressor Proteins
  • Tetracycline

Identity

Scopus Document Identifier

  • 0032486128

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1998.1775

PubMed ID

  • 9642048

Additional Document Info

volume

  • 279

issue

  • 2