Structural analysis and phylogenetic implication of MreB protein in Aeromonas veronii

Abstract:

[Objective] To understand all-level structures of Aeromonas veronii MreB protein, and study the conservation of MreB protein and its reliability as a molecular marker. [Methods] Online software such as ProtParam, PredictProtein and SWISS-MODEL were used to analyze the primary structure and physicochemical properties of the protein, and predict its secondary and tertiary structures. Amino acid sequence comparative analysis and phylogenetic study were done on MreB proteins in several types of bacteria through software like ClustalX 2.0, ESpript 3.0 and MEGA 6. [Results] MreB protein of Aeromonas veronii is an acidic protein composed of 346 amino acids, which is mainly located in the cell membrane. Secondary structure of the protein mainly consists of α-helices, extended long chains and random coil structures, of which random coils share the highest proportion. The results of homology modeling reveal that the tertiary structure of the protein contains 12 α-helical structures, 5 β-folded structures, 8 β-hairpin structures, 22 β-turns and 4 γ-turns. [Conclusion] Detailed physicochemical information on Aeromonas veronii MreB protein is obtained. The model built by homology modeling presents a reasonable spatial structure, and receives a relatively high PROCHECK score, which provides some structural basis for experimental research. Moreover, with conserved sites and structural conservation, MreB protein belongs to a highly conserved protein with appropriate variability. Therefore, it can be used as a molecular marker tool in the classification and identification of bacteria.