Professor Shi Yigong, who graduated from Tsinghua University in the early years, has attracted the attention of all parties since returning to China. Although he has experienced a lot of public opinion controversy, he still walked out of his own path in the academic field. Gong published 12 papers in top international journals such as Nature, and the frequency of high-level results is higher than when he was abroad. At the same time, he also built a talent introduction bridge centered on Tsinghua University.
Secondary active transport (Secondary active transport), also known as cotransport, refers to a substance that can reverse the concentration difference for transmembrane transport, but its energy does not come from ATP decomposition, but is caused by the high transport of other substances. The transport mode provided by potential energy. The potential energy reserve formed by the secondary active transport activity can also be used to complete the transmembrane transport of the reverse concentration difference of some other substances, such as the absorption of glucose, amino acids and other nutrients by the intestinal epithelial and renal tubular epithelial cells.
The sequences of transporters with different functions found in the current research are usually not similar, but some scientists have found that these action factors have similar folds, such as MFS, LeuT, and NhaA folds.
The researchers analyzed multiple conformational states of the same transport family, such as members of the LeuT superfamily MHP1, ADIC, vSGLT, LeuT, and found that there is a close relationship between structural changes and substrate binding and transport. Despite recent achievements in biochemistry and structure, scientists do not know much about the recognition of these substrates and their energy coupling. This review focuses on the common folding of secondary active transport elements and the common transport mechanism. Through some structural information, the mechanism of action related to newly discovered structure, biochemical and computational simulation evidence is analyzed.
Previously, the research team led by Professor Shi Yigong had analyzed the three-dimensional structure of the energy coupling factor transporter by X-ray crystal diffraction. By analyzing the structure of the protein, the researchers found that the membrane protein EcfS is basically parallel to the cell membrane, while the general membrane protein is basically perpendicular to the cell membrane. Based on this extremely special conformation, the researchers believe that the transporter EcfS takes up the substrate by flipping inside the membrane. When it is in the state of vertical cell membrane, EcfS can combine with the substrate, then flip into parallel state and release the substrate, and then return to the vertical state for the next round of circulation, similar to the wine glass in the vertical state after receiving water, then flipping out Water in the glass. In this process, the hydrophilic proteins EcfA and EcfA 'hydrolyze ATP and couple to the membrane protein EcfT to provide energy for the inversion of EcfS. This transport mode is different from the current "alternating access" model for transport proteins. It is a new working model of membrane transport proteins.
This is another major breakthrough in the research of energy-coupling factor transporter after Professor Shi Yigong's research team first analyzed and reported the crystal structure of membrane protein EcfS in the world in 2010.
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