Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli

被引:0
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作者
Chih-Chia Su
Feng Long
Michael T. Zimmermann
Kanagalaghatta R. Rajashankar
Robert L. Jernigan
Edward W. Yu
机构
[1] Iowa State University,Department of Chemistry
[2] Iowa State University,Bioinformatics and Computational Biology Interdepartmental Graduate Program
[3] Cornell University,NE
[4] Building 436E,CAT and Department of Chemistry and Chemical Biology
[5] Argonne National Laboratory,Department of Biochemistry
[6] Biophysics and Molecular Biology,Department of Physics and Astronomy
[7] Iowa State University,undefined
[8] Iowa State University,undefined
来源
Nature | 2011年 / 470卷
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摘要
Gram-negative bacteria expel toxic chemicals through tripartite efflux pumps spanning both the inner and outer membranes. A crystallographic model of this tripartite efflux complex has been unavailable because co-crystallization of different components of the system has proved extremely difficult. The X-ray crystal structure of the CusA/CusB co-complex from Escherichia coli has now been determined. The structure reveals that the trimeric CusA efflux pump interacts with six CusB protein molecules at the upper half of the periplasmic domain, and the predicted structure of the trimeric CusC channel was used to develop a model of the tripartite efflux complex.
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页码:558 / 562
页数:4
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