Structure Prediction and Binding Site Analysis of Hepatotoxic Microcystin-LR Degrading MlrC-Like Protein from <i>Burkholderia</i> sp. using Computational Approaches

Abstract

Microcystin-LR (MCYST-LR) is a well characterized hepatotoxic heptapeptide produced by various species of cyanobacteria including Microcystis aeruginosa. Burkholderia is a genus of bacteria with cyanobacterial toxins degrading property. This study predicts the structure of microcystin degrading MlrC-like protein from Burkholderia sp. strain CCGE1002 that has microcystin degradation capability. Binding interaction of MlrC-like protein with MCYST-LR was studied. Threedimensional model of MlrC-like protein was generated using composite modeling based I-TASSER server. The model was further assessed through different computational approaches. The generated model was found comparable to experimental structures. MCYST-LR was used for docking with predicted model to investigate ligand-protein interaction. The study provides the structural insight into the binding mode of MlrC-like protein of Burkholderia sp. with MCYST-LR and could be further helpful in designing modeling inhibitors for MCYST-LR.

Proteomic Profile of the Toxic Cyanobacteria Microcystic aeruginosa

“…et al(2016), the common structure of the microcystin heptapeptide is cyclo (D-Ala1 -Xxx 2 -D-MeAsp 3 -Zzz 4 -Adda 5 -D-Glu6 -Mdha 7 ), where Xxx and Zzz represent highly variable L-amino acids at positions 2 and 4 of the cyclic peptide, D-MeAsp 3 is D-erythro-β-Adda 5 is 3-amino-9methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid. Also, there exists a desmethyl derivative bearing D-Asp 3 .…”

“…Also, there exists a desmethyl derivative bearing D-Asp 3 . Singh et al(2016) have described the chemical structure of microcystin-LR (Fig.3B) where two amino acids, arginine, and leucine, are occupying.…”