Structural changes and binding characteristics of the tetracycline-repressor binding site on induction

Harald Lanig; Olaf G Othersen; Ute Seidel; Frank R Beierlein; Thomas E Exner; Timothy Clark

doi:10.1021/jm060289g

Structural changes and binding characteristics of the tetracycline-repressor binding site on induction

J Med Chem. 2006 Jun 15;49(12):3444-7. doi: 10.1021/jm060289g.

Authors

Harald Lanig¹, Olaf G Othersen, Ute Seidel, Frank R Beierlein, Thomas E Exner, Timothy Clark

Affiliation

¹ Computer-Chemie-Centrum der Universität Erlangen-Nürnberg, Nägelsbachstrasse 25, 91052 Erlangen, Germany.

PMID: 16759085
DOI: 10.1021/jm060289g

Abstract

The binding motif (pharmacophore) for induction and the changes in the structure of the binding site that accompany induction have been determined from molecular-dynamics simulations on the tetracycline-repressor signal-transduction protein. The changes and the induction mechanism are discussed and compared with conclusions drawn from earlier X-ray structures. The differences in inducer strength of tetracycline and 5a,6-anhydrotetracycline are discussed with respect to their interaction in the MD simulations.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Allosteric Regulation
Anti-Bacterial Agents / chemistry
Binding Sites
Crystallography, X-Ray
Models, Molecular*
Protein Binding
Protein Conformation
Protein Synthesis Inhibitors / chemistry
Repressor Proteins / biosynthesis
Repressor Proteins / chemistry*
Tetracycline / chemistry
Tetracyclines / chemistry*

Substances

Anti-Bacterial Agents
Protein Synthesis Inhibitors
Repressor Proteins
Tetracyclines
tetracycline resistance-encoding transposon repressor protein
4-epianhydrotetracycline
Tetracycline