Structural and functional analysis of Bradyrhizobium yuanmingense and Rhizobium tropici nifA proteins: Insights into physicochemical properties and domain architecture

Abstract

There are two key proteins, A0A844SEK3_9BRAD and A0A6P1CI42_RHITR, from Bradyrhizobium yuanmingense and Rhizobium tropici strain CIAT 899, respectively that are known to play an important role in symbiotic relationships with legumes and nitrogen fixation. Studying these proteins mechanism is essential for advancing agricultural practices. This study aims to provide insights into their structural features. The analysis of the physicochemical properties of the proteins revealed their molecular weights, theoretical isoelectric points, and amino acid compositions. Secondary structure analysis predicted the presence of alpha helices, extended strands, and random coils in both proteins, indicating diverse structural compositions that contribute to their overall architecture and potential functions. Tertiary structure prediction provided insights into the three-dimensional arrangement of the proteins, with models exhibiting moderate to good quality and high structural similarity to the templates. Domain analysis identified distinct domains within the proteins, and Nif-specific regulatory protein domains, which shed light on their functional characteristics. The presence of specific domains in the proteins suggests their involvement in ATP binding, signal transduction, DNA binding, and transcriptional regulation.
The structural and functional characteristics of A0A844SEK3_9BRAD and A0A6P1CI42_RHITR are thoroughly understood in this study, which advances our understanding of nitrogen fixation and plant-microbe relationships. The results have implications for optimizing agricultural practices.