【摘 要】
：
The bacterial phosphoenolpyruvate (PEP): carbohydrate phosphotransferase system (PTS) is a unique sugar uptake pathway.Sugar transport is accomplished by three components of the system: Enzyme Ⅰ (EⅠ),
【机 构】
：
Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX
【出 处】
：
The 9th Asian Biophysics Association Symposium (ABA2015)(第九届
论文部分内容阅读
The bacterial phosphoenolpyruvate (PEP): carbohydrate phosphotransferase system (PTS) is a unique sugar uptake pathway.Sugar transport is accomplished by three components of the system: Enzyme Ⅰ (EⅠ), the histidine-containing phosphocarrier protein (HPr) and Enzyme Ⅱ Complex (EⅡ), which is composed of protein subunits EllA, B and C.An extracellular sugar molecule is taken up by EⅡC, translocated across the cell membrane so that it is accessible from the intracellular side, and phosphorylated by EⅡB before it is released into the cytosol.The phosphate group originates from PEP, and is transferred sequentially through EⅠ, HPr, EⅡA and EⅡB.Covalent modification of the sugar during transport, known as group translocation, makes the mechanism of EⅡC distinct from that of other families of sugar transporters.Full understanding of this mechanism has been hampered by the lack of atomic resolution crystal structures of EⅡC.We have solved crystal structures of two EⅡC homologs from Bacillus cereus, and by comparing the two structures we were able to deduce conformational changes required for substrate translocation and phosphorylation.
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