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Published Online August 23, 2007
Science DOI: 10.1126/science.1143748

Reports

Submitted on April 12, 2007
Accepted on August 7, 2007

Structure of the Zinc Transporter YiiP

Min Lu 1 and Dax Fu 1*

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

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

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 signalling. Here, we report the x-ray structure of YiiP in complex with zinc at 3.8 Å 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, while 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.


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