Structural Dynamic of FLS2 LRR D122N BAK1 LRR Crystal Complex

Abstract

This study includes a protein subunit extraction from Arabidopsis Thaliana. Arabidopsis Thaliana, an ideal plant for any type of research leading to a new direction of genetic experiments. Its importance shows by its minimum size that restrict the need of growth facilities, self-pollination that speeds the seed production. A mutation in the third leucine repeat of the BRI1 linked kinase 1(BAK1) protein of 4mn8 in Arabidopsis Thaliana changes the 122nd amino acid which is aspartate to asparagine along with deleted flg22.The mutation is specifically associated with photo morphogenesis. The BAK1 enzyme, however, also plays a key role in plant immunity by producing a heterodimer with a pattern-triggered flagellin sensing 2 (FLS2) receptor, a bacterial flagellin elicitor protein that leads to BAK1 and FLS2 trans-phosphorylation and subsequent initiation of the signal transduction pathway which is involve in activation of the immune response. The impact of the D122N mutation in BAK1 on the structural integrity of the FLS2-BAK1 complex was investigated here through molecular dynamics simulation. The D122N mutation in the native FLS2-BAK1 crystallographic structure of the BAK1 protein was induced using the in silico process. Simulation was done for both native and mutant complexes by subsequently utilizing molecular dynamics techniques for 5ns.The mutant and native complex is compared based on some parameters like RMSD (Root Mean Square Deviation), RMSF (Root Mean Square Fluctuation), Rg (Radius of Gyration), Hydrogen bond etc. The mutation is found to result in lower deviation of atoms from reference structure for the whole complex, FLS2- BAK1, compared to counterpart from the non-mutated complex. RMSF analysis revealed that mutation caused lower fluctuation of amino acid in both the N terminal and C terminal of FLS2- BAK1 complex that hinder stable interactions.FLS2-BAK1 had a lower radius of gyration at the complex containing mutation compared to the non-mutated complex. The mutation hindered the viii formation of hydrogen bonds among all the peptides, often terminating all the hydrogen bonds between peptide.