The purpose of this study is to mimic the three-dimensional (3D) structures of the main subunit (CstH) and chaperone (CS3-1) of CS3 pili using computational techniques, namely comparative protein modelling. Pili or fimbriae are surface hair-like structures produced by Gram negative bacteria. Models for CstH and CS3-1 were created and submitted in the PMDB database under the ID codes PM0079873 and PM0078481, respectively. 3D structures were used in the molecular dimerization to find possible interaction sites in the CstH molecule. The interaction surface areas of dimer molecules were calculated using the PDBePISA system. The interaction affinities and electrostatic potential of the CstH subunit surfaces and complexes were determined using the PPEPred server and APBS software, respectively. The results demonstrated that analysing 3D models provides great insight into the permissive sites, binding mode, and contact sites of the CstH protein, and that our method could be relevant in future experimental study on pili biology and applications.
Author(S) Details
Vajiheh Eskandari
Department of Biology, Faculty of Science, University of Zanjan, Zanjan, Iran.
Bagher Yakhchali
National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran.
Seyed Shahriar Arab
Department of Biophysics, Faculty of Biological Science, Tarbiat Modarres University, Tehran, Iran.
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