Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051903 | FEBS Letters | 2006 | 6 Pages |
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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Authors
N. Hanekop, J. Zaitseva, S. Jenewein, I.B. Holland, L. Schmitt,