Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport

Feng Long, Chih-Chia Su, Michael T. Zimmermann, Scott E. Boyken, Kanagalaghatta R. Rajashankar, Robert L. Jernigan and Edward W. Yu ()
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Feng Long: Molecular, Iowa State University
Chih-Chia Su: Iowa State University
Michael T. Zimmermann: Iowa State University
Scott E. Boyken: Iowa State University
Kanagalaghatta R. Rajashankar: Cornell University, Building 436E, Argonne National Laboratory
Robert L. Jernigan: Iowa State University
Edward W. Yu: Molecular, Iowa State University

Nature, 2010, vol. 467, issue 7314, 484-488

Abstract: Methionine-aided metal transport Gram-negative bacteria, such as Escherichia coli, use tripartite efflux complexes in the resistance-nodulation-division family to expel diverse toxic compounds from the cell. The CusCBA system is responsible for extruding biocidal Cu(I) and Ag(I) ions from the cell. The X-ray crystal structure of CusA, the inner membrane transporter, has now been determined in the absence and presence of bound Cu(I) or Ag(I). The structures suggest that the metal binding site, formed by a three-methionine cluster, is located within the cleft region of the periplasmic domain. The authors propose a potential pathway for ion export in which CusA is capable of picking up the metal ion from the cytosol, with this transporter utilizing the methionine pairs and clusters to bind and export metal ions.

Date: 2010
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DOI: 10.1038/nature09395

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