Use of molecular dynamics with a distance constraint to investigate the transition pathway of the FixJ receiver domain

 

Philippe Roche§, Liliane Mouawad, David Perahia, Jean-Pierre Samama and Daniel Kahn

 

§Division of Structural Biology, University of Oxford, Henry Wellcome Building for Genomic Medicine, Roosevelt Drive, Oxford, OX3 7BN, UK.

 

 

 

FixJ is a two domain response regulator involved in nitrogen fixation in Sinorhizobium meliloti. Recent X-ray characterization of both the native (unphosphorylated) and the active (phosphorylated) states of the protein identify conformational changes of the b4-a4 loop and the conserved residue Phe101 as the key switches in activation[1]1,2. These structures also allowed investigation of the transition between conformations of this two-component regulatory receiver domain by molecular dynamics simulations. The path for the conformational change was studied with a distance constraint directing the system from one state to the other (“Path Exploration with Distance Constraints” procedure 3). The simulations provide evidence for a correlation between the conformation of the b4-a4 loop and the orientation of the conserved residue Phe101 (*). From these simulations, a model presenting the sequence of events during the activation/deactivation process was proposed 4.

 

 



[1]1.- Birck, C., Mourey, L., Gouet, P., Fabry, B., Schumacher, J., Rousseau, P., Kahn, D., and Samama, J.P. 1999. Conformational changes induced by phosphorylation of the FixJ receiver domain. Structure Fold Des. 7: 1505-1515.

2.- Gouet, P., Fabry, B., Guillet, V., Birck, C., Mourey, L., Kahn, D., and Samama, J.P. 1999. Structural transitions in the FixJ receiver domain. Structure Fold Des. 7: 1517-1526.

3.- Guilbert, C., Perahia, D., and Mouawad, L. 1995. A method to explore transition paths in macromolecules. Applications to hemoglobin and phosphoglycerate kinase. Computer Phys. Comm. 91: 263-274.

4.- Roche, P., Mouawad, L., Perahia, D., Samama, J.P. and Kahn D. 2002. Molecular dynamics of the FixJ receiver domain: Movement of the b4-a4 loop correlates with the in and out flip of Phe101. Protein Sci. 11: 2622-2630.

(*) Movie presentations of representative trajectories can be found at the URL

http://www.toulouse.inra.fr/lbmrpm/dk/Fixj_index.html .