Molecular Dynamics Simulations of the Tetracycline-repressor Protein: The Mechanism of Induction. Export

@article{citeulike:634916, abstract = {Molecular dynamics simulations on the tetracycline-repressor (TetR) protein, both in the absence of an inducer and complexed with the inducers tetracycline and 5a,6-anhydrotetracycline, show significant differences in the structures and dynamics of the induced and non-induced forms of the protein. C(alpha)-density-difference plots, low-frequency normal vibrations and inter-residue interaction energies all point to a common mechanism of induction. The inducer displaces Asp156 from the magnesium ion in the binding pocket, leading to a short cascade of rearrangements of salt bridges that results in the allosteric change. The increased flexibility of the induced form of the protein is suggested to contribute to the decrease in binding affinity to DNA on induction.}, address = {Computer-Chemie-Centrum der Friedrich-Alexander-Universit\"{a}t Erlangen-N\"{u}rnberg, N\"{a}gelsbachstrasse 25, 91052 Erlangen, Germany.}, author = {Lanig, Harald and Othersen, Olaf G G. and Beierlein, Frank R R. and Seidel, Ute and Clark, Timothy}, citeulike-article-id = {634916}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.jmb.2006.04.014}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16690082}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16690082}, day = {27}, doi = {10.1016/j.jmb.2006.04.014}, issn = {0022-2836}, journal = {J Mol Biol}, keywords = {md, simulation}, month = {April}, posted-at = {2006-05-15 03:20:27}, priority = {2}, title = {Molecular Dynamics Simulations of the Tetracycline-repressor Protein: The Mechanism of Induction.}, url = {http://dx.doi.org/10.1016/j.jmb.2006.04.014}, year = {2006} }

TY - JOUR ID - citeulike:634916 L3 - citeulike-article-id:634916 N2 - Molecular dynamics simulations on the tetracycline-repressor (TetR) protein, both in the absence of an inducer and complexed with the inducers tetracycline and 5a,6-anhydrotetracycline, show significant differences in the structures and dynamics of the induced and non-induced forms of the protein. C(alpha)-density-difference plots, low-frequency normal vibrations and inter-residue interaction energies all point to a common mechanism of induction. The inducer displaces Asp156 from the magnesium ion in the binding pocket, leading to a short cascade of rearrangements of salt bridges that results in the allosteric change. The increased flexibility of the induced form of the protein is suggested to contribute to the decrease in binding affinity to DNA on induction. JF - J Mol Biol SN - 0022-2836 AD - Computer-Chemie-Centrum der Friedrich-Alexander-Universität Erlangen-Nürnberg, Nägelsbachstrasse 25, 91052 Erlangen, Germany. TI - Molecular Dynamics Simulations of the Tetracycline-repressor Protein: The Mechanism of Induction. KW - md KW - simulation AU - Lanig, Harald AU - Othersen, Olaf G AU - Beierlein, Frank R AU - Seidel, Ute AU - Clark, Timothy PY - 2006/04/27/ UR - http://dx.doi.org/10.1016/j.jmb.2006.04.014 ER -