Molecular insights into the mechanism of ATP-hydrolysis by the NBD of the ABC-transporter HlyB |
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Authors: | Hanekop N Zaitseva J Jenewein S Holland I B Schmitt L |
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Affiliation: | Institute of Biochemistry, Heinrich Heine University Duesseldorf, Universitaetsstr. 1, 40225 Duesseldorf, Germany. |
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Abstract: | The ABC-transporter HlyB is a central element of the Type I protein secretion machinery, dedicated to export the E. coli toxin HlyA in a single step across the two membranes of the cell envelope. Here, we discuss recent insights into the structure and the mechanism of ATP-hydrolysis by the NBD of HlyB. Combining structural and biochemical data, we have suggested that substrate-assisted catalysis (SAC), but not general base catalysis, is responsible for ATP-hydrolysis in this NBD and might also operate in other NBDs. Finally, the implications and advantages of SAC are discussed in the context of ATP-induced dimerization of the NBDs. |
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Keywords: | ABC, ATP-binding cassette Hly, haemolysin NBD, nucleotide-binding domain SAC, substrate-assisted catalysis TMD, transmembrane domain |
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