A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation.
A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation.
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DOI:
10.1038/nsmb.1770
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发表时间:
2010-03
影响因子:
16.8
通讯作者:
中科院分区:
文献类型:
--
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ATP binding cassette (ABC) transporters are integral membrane proteins that translocate a diverse array of substrates across cell membranes. We present here the dynamics of complex formation of three structurally characterized ABC transporters: the BtuCD vitamin B12 importer and MetNI D/L-methionine importer from Escherichia coli, and the Haemophilus influenzae Hi1470/1 metal-chelate importer, with their cognate binding proteins. Similar to other ABC importers, MetNI interacts with its binding protein with low affinity (Kd ~ 10-4 M). In contrast, BtuCD-F and Hi1470/1-2 form stable, high affinity complexes (Kd ~ 10-13 and 10-9 M, respectively). In BtuCD-F, vitamin B12 accelerates complex dissociation rate ~107-fold, with ATP having an additional destabilizing effect. The findings presented here highlight substantial mechanistic differences between BtuCD-F, and likely Hi1470/1-2, and the better characterized maltose and related ABC transport systems, indicating considerable mechanistic diversity within this large protein super-family.
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影响因子:
56.9
作者:
Locher, KP;Lee, AT;Rees, DC
通讯作者:
Rees, DC
影响因子:
3.2
作者:
BASSFORD, PJ;KADNER, RJ
通讯作者:
KADNER, RJ
影响因子:
3.2
作者:
Cadieux, N;Bradbeer, C;Kadner, RJ
通讯作者:
Kadner, RJ
影响因子:
4.8
作者:
Ames, GFL;Liu, CE;Nikaido, K
通讯作者:
Nikaido, K
DOI:
10.1126/science.1157987
发表时间:
2008-07-11
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Kadaba NS;Kaiser JT;Johnson E;Lee A;Rees DC
通讯作者:
Rees DC