Structural changes and binding characteristics of the tetracycline-repressor binding site on induction.
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.
Lanig
Harald
H
Computer-Chemie-Centrum der Universität Erlangen-Nürnberg, Nägelsbachstrasse 25, 91052 Erlangen, Germany.
Othersen
Olaf G
OG
Seidel
Ute
U
Beierlein
Frank R
FR
Exner
Thomas E
TE
Clark
Timothy
T
D000494:Allosteric Regulation; D000900:Anti-Bacterial Agents / Q000737:chemistry; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011500:Protein Synthesis Inhibitors / Q000737:chemistry; D012097:Repressor Proteins / Q000096:biosynthesis / Q000737:chemistry*; D013752:Tetracycline / Q000737:chemistry; D013754:Tetracyclines / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D011500:Protein Synthesis Inhibitors; D012097:Repressor Proteins; D013754:Tetracyclines; C034811:tetracycline resistance-encoding transposon repressor protein; C016229:4-epianhydrotetracycline; D013752:Tetracycline