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Journal article

Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC.

Abstract:

The trimeric TolC protein of Escherichia coli comprises an outer membrane beta-barrel and a contiguous alpha-helical barrel projecting across the periplasm. This provides a single 140 A long pore for multidrug efflux and protein export. We have previously reported that trivalent cations such as hexammine cobalt can severely inhibit the conductivity of the TolC pore reconstituted in planar lipid bilayers. Here, isothermal calorimetry shows that Co(NH(3))(6)(3+) binds to TolC with an affinity o...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2004.07.088

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Journal:
Journal of molecular biology More from this journal
Volume:
342
Issue:
3
Pages:
697-702
Publication date:
2004-09-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:196859
UUID:
uuid:6b5e6169-2b32-4ca2-80d9-667a7f80cd09
Local pid:
pubs:196859
Source identifiers:
196859
Deposit date:
2012-12-19

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