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

被引:50
作者
Hanekop, N
Zaitseva, J
Jenewein, S
Holland, IB
Schmitt, L
机构
[1] Univ Dusseldorf, Inst Biochem, D-40225 Dusseldorf, Germany
[2] Univ Paris 11, Inst Genet & Microbiol, Orsay, France
来源
FEBS LETTERS | 2006年 / 580卷 / 04期
关键词
ABC-transporters; dimerization; nucleotide-binding domain; substrate-assisted catalysis; crystal structures;
D O I
10.1016/j.febslet.2005.11.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1036 / 1041
页数:6
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