2NS7

How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor

Summary for 2NS7

• Entry DOI: 10.2210/pdb2ns7/pdb
• Related: 1QPI 2NS8 2TCT
• Descriptor: Tetracycline repressor protein (1 entity in total)
• Functional Keywords: transcription regulator, helix-turn-helix, transcription
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 94126.65

Authors

Luckner, S.R.,Klotzsche, M.,Berens, C.,Hillen, W.,Muller, Y.A. (deposition date: 2006-11-03, release date: 2007-07-24, Last modification date: 2023-10-25)

Primary citation

Luckner, S.R.,Klotzsche, M.,Berens, C.,Hillen, W.,Muller, Y.A.
How an agonist peptide mimics the antibiotic tetracycline to induce Tet-repressor
J.Mol.Biol., 368:780-790, 2007

PubMed Abstract: A 16-residue peptide, called Tip, induces the tetracycline repressor TetR as efficiently as the antibiotic tetracycline when fused to the N or C terminus of another protein. This is unusual because the majority of in vitro selected peptides, such as Tip, inhibit protein function, and agonist peptides are only rarely identified. We elucidated the atomic mechanism of TetR induction by Tip from crystal structures of TetR in complex with Tip and of free TetR. Peptide induction ultimately results in the same movements of DNA reading heads, but Tip accomplishes this by very different molecular interactions from tetracycline involving important contacts to the TetR surface. As a direct consequence, an alternate pathway of allostery becomes possible that makes ample use of intersubunit interactions. For the first time it is possible to show in atomic detail how a small molecule controlled bacterial transcription factor such as TetR becomes responsive to protein-protein interactions, characteristic of gene transcription regulation in higher organisms.

PubMed: 17374541
DOI: 10.1016/j.jmb.2007.02.030

Experimental method

X-RAY DIFFRACTION (2.4 Å)