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Heavy metal transport by the C us CFBA efflux system
Author(s) -
Delmar Jared A.,
Su ChihChia,
Yu Edward W.
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2764
Subject(s) - efflux , periplasmic space , inner membrane , bacterial outer membrane , membrane transport protein , transport protein , transporter , escherichia coli , bacteria , biology , multidrug resistance associated proteins , membrane protein , biochemistry , membrane transport , microbiology and biotechnology , chemistry , atp binding cassette transporter , biophysics , membrane , genetics , gene
It is widely accepted that the increased use of antibiotics has resulted in bacteria with developed resistance to such treatments. These organisms are capable of forming multi‐protein structures that bridge both the inner and outer membrane to expel diverse toxic compounds directly from the cell. Proteins of the resistance nodulation cell division (RND) superfamily typically assemble as tripartite efflux pumps, composed of an inner membrane transporter, a periplasmic membrane fusion protein, and an outer membrane factor channel protein. These machines are the most powerful antimicrobial efflux machinery available to bacteria. In Escherichia coli, the CusCFBA complex is the only known RND transporter with a specificity for heavy metals, detoxifying both Cu + and Ag + ions. In this review, we discuss the known structural information for the CusCFBA proteins, with an emphasis on their assembly, interaction, and the relationship between structure and function.