Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 426, Issue 2, Pages 403-411Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2013.09.042
Keywords
outer membrane channel; beta-barrel membrane protein; heavy-metal resistance; resistance-nodulation-cell division
Categories
Funding
- National Institutes of Health [R01GM086431]
- National Center for Research Resources at the National Institutes of Health [RR-15301]
- U.S. Department of Energy, Office of Basic Energy Sciences [DE-AC02-06CH11357]
- Science Undergraduate Laboratory Internship (SULI) from the DOE
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Gram-negative bacteria, such as Escherichia coli, frequently utilize tripartite efflux complexes in the RND (resistance-nodulation-cell division) family to expel diverse toxic compounds from the cell. These complexes span both the inner and outer membranes of the bacterium via an a-helical, inner membrane transporter; a periplasnnic membrane fusion protein; and a beta-barrel, outer membrane channel. One such efflux system, CusCBA, is responsible for extruding biocidal Cu(I) and Ag(I) ions. To remove these toxic ions, the CusC outer membrane channel must form a beta-barrel structural domain, which creates a pore and spans the entire outer membrane. We here report the crystal structures of wild-type CusC, as well as two CusC mutants, suggesting that the first N-terminal cysteine residue plays an important role in protein membrane interactions and is critical for the insertion of this channel protein into the outer membrane. These structures provide insight into the mechanisms on CusC folding and transmembrane channel formation. It is found that the interactions between CusC and membrane may be crucial for controlling the opening and closing of this beta-barrel, outer membrane channel. (C) 2013 Elsevier Ltd. All rights reserved.
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