Comparative structural analysis of two proteins belonging to quorum sensing system in Vibrio cholerae.
Vibrio cholerae uses quorum sensing communication system to interact with other bacteria and for gauzing environmental parameters. This organism dwells equally well in both human host and aquatic environments. Quorum sensing regulates multitude of activities and is one of the lucrative targets presently pursued for drug design in bacteria to encounter virulence. Histidine phosphotransfer protein LuxU and response regulator LuxO of V. cholerae are known to play important roles in biofilms and virulence machinery. In the present study, we used computational methods to model LuxU and LuxO and simulated the interactions of LuxO and LuxU. Since no structural details of the proteins were available, we employed homology modeling to construct the three-dimensional structures and then performed molecular dynamics simulations to study dynamic behavior of the LuxO and LuxU from V. cholerae. The modeled proteins were validated and subjected to molecular docking analyses. This allowed us to predict the binding modes of the proteins to elucidate probable sites of interference.
Infectious Disease Biology, Institute of Life Sciences, Nalco Square, Bhubaneswar 751023, India.
Mobashar Hussain Urf Turabe
MH
Fazil
Sunil
S
Kumar
Naidu Subba
NS
Rao
Chandrabose
C
Selvaraj
Sanjeev Kumar
SK
Singh
Haushila Prasad
HP
Pandey
Durg Vijai
DV
Singh
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018441:Biofilms; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D053038:Quorum Sensing; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism; D015398:Signal Transduction; D014734:Vibrio cholerae / Q000378:metabolism*
D001426:Bacterial Proteins; C088907:LuxO protein, Vibrio harveyi; C117251:LuxU protein, Vibrio; D010750:Phosphoproteins; D012097:Repressor Proteins