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the Chinese Academy of Sciences Biomedical Research Group published the new findings

2014-07-29 来源:转载自第三方

Many of the key physiological activities by the cell membrane transport protein tomediate many physiological activities, cannot do without transporter, such as celland the outside of the substance information exchange, metabolites, nutrient absorption and secretion. These transporters is composed of primary activetransporters and secondary transporters.

MFS (mainly assist transporter superfamily) is a typical representative ofsecondary transporters, rely on the proton electrochemical gradient as a variety of substrates or driving force transfer including small molecules, peptides. MFS plays a key role in cell of material exchange and energy metabolism, protondependent peptide transporter of (POT) is an important class of MFS. As with other MFS, POT proteins need to convert between the two main conformations in the transport of substrates. The 12 transmembrane helical prokaryotic POT has a classic, transmembrane core is also divided into two domains, twotransmembrane helices are inserted in between the two domains.

Through their crystal structure reveals conformational YbgH oriented cells, also analyzed the key parts of the conformational change of protein stability and regulation. The results were presented on July 24th at Cell's Structure magazine.Research shows, the central cavity in the form of protein, amino acid conserved residue Glu21 is critical to transfer function, which is the substrate binding site ofprotonation induced.

Research shows, the central cavity in the form of protein, amino acid conserved residue Glu21 is critical to transfer function, which is the substrate binding site ofprotonation induced. Motif A as the switch of conformational transitions, stable YbgH for extracellular state. And between the two domains of transmembranehelix, is also very important for protein translocation activity.

The researchers said: the two main conformations of POT protein, their balancein this study is the key to its transport activity.


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