It was learned from Tsinghua University that Shi Yigong, a professor of the school ’s School of Life Sciences, published a research paper entitled "Bacteria Energy Coupling Factor Transporter Structure" online in the journal Nature on the 14th and reported for the first time the energy coupling factor transporter complex The crystal structure of the tetramer and the working molecular mechanism of the protein complex are explained by the structural information.
Energy-coupled transport proteins are a class of newly identified transport proteins in recent years. They are widely present in Gram-positive pathogens and are responsible for ingesting some vitamins and other trace elements.
After nearly three years of unremitting efforts, the research team led by Shi Yigong analyzed the three-dimensional structure of the energy coupling factor transporter by X-ray crystal diffraction. This transport mode is different from the current general model for transport proteins and is a new working model of membrane transport proteins.
This is another major breakthrough for the research team of Shi Yigong after studying and reporting the crystal structure of membrane proteins in the world for the first time in 2010. According to information provided by Tsinghua University, since the transport protein only exists in bacteria, new antibacterial drugs can be screened or designed for such proteins. Therefore, this work is not only a breakthrough in explaining the working mechanism of the energy coupling factor transporter, but also has a reference value for solving the increasingly serious problems of bacterial resistance.
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