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Science 317 (5845): 1746-1748

Copyright © 2007 by the American Association for the Advancement of Science

Structure of the Zinc Transporter YiiP

Min Lu, and Dax Fu*

Abstract: YiiP is a membrane transporter that catalyzes Zn2+/H+ exchange across the inner membrane of Escherichia coli. Mammalian homologs of YiiP play critical roles in zinc homeostasis and cell signaling. Here, we report the x-ray structure of YiiP in complex with zinc at 3.8 angstrom resolution. YiiP is a homodimer held together in a parallel orientation through four Zn2+ ions at the interface of the cytoplasmic domains, whereas the two transmembrane domains swing out to yield a Y-shaped structure. In each protomer, the cytoplasmic domain adopts a metallochaperone-like protein fold; the transmembrane domain features a bundle of six transmembrane helices and a tetrahedral Zn2+ binding site located in a cavity that is open to both the membrane outer leaflet and the periplasm.

Department of Biology, Brookhaven National Laboratory, Upton, NY 11973, USA.

* To whom correspondence should be addressed. E-mail: dax{at}bnl.gov

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