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Molecular insights into the mechanism of ATP-hydrolysis by the NBD of the ABC-transporter HlyB

期刊

FEBS LETTERS
卷 580, 期 4, 页码 1036-1041

出版社

WILEY
DOI: 10.1016/j.febslet.2005.11.012

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ABC-transporters; dimerization; nucleotide-binding domain; substrate-assisted catalysis; crystal structures

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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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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