Abstract
TbpA is a highly conserved transmembrane protein that may serve as a channel for transport of iron across the outer membrane, which is required for transferrin utilization and is responsible for removing the iron from transferrin and for transporting iron across the outer membrane in a TonB-dependent manner. In the present study, a 3D homology modeling of TbpA from Actinobacillus pleuropneumoniae (App) L20 strain, based upon the Crystal structure of the hemehemoglobin outer membrane transporter ShuA from Shigella dysenteriae (PDB code: 3fhh) was performed using bioinformatics tools, as no experimental 3D structures. The program VERIFY 3D assessed the quality of the predicted structure of TbpA with acceptable scores. All the results converged to the fact that the predicted 3-Dimenrsional structure of TbpA is of good quality with acceptable scores.
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