| Title | Conformational changes of the Tet repressor induced by tetracycline trapping. |
| Publication Type | Journal Article |
| Year of Publication | 1998 |
| Authors | Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W |
| Journal | J Mol Biol |
| Volume | 279 |
| Issue | 2 |
| Pagination | 439-47 |
| Date Published | 1998 Jun 05 |
| ISSN | 0022-2836 |
| Keywords | Amino Acid Sequence, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Escherichia coli, Gene Expression Regulation, Bacterial, Models, Molecular, Molecular Sequence Data, Mutation, Protein Conformation, Protein Structure, Secondary, Recombinant Fusion Proteins, Repressor Proteins, Tetracycline, Water |
| 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. |
| DOI | 10.1006/jmbi.1998.1775 |
| Alternate Journal | J Mol Biol |
| PubMed ID | 9642048 |
Submitted by jom4013 on December 3, 2020 - 4:05pm