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Originally published in Science Express on 23 August 2007
Science 21 September 2007:
Vol. 317. no. 5845, pp. 1746 - 1748
DOI: 10.1126/science.1143748
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Reports

Structure of the Zinc Transporter YiiP

Min Lu and Dax Fu*

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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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Glutathione and Transition-Metal Homeostasis in Escherichia coli.
K. Helbig, C. Bleuel, G. J. Krauss, and D. H. Nies (2008)
J. Bacteriol. 190, 5431-5438
   Abstract »    Full Text »    PDF »
Deletion of a Histidine-rich Loop of AtMTP1, a Vacuolar Zn2+/H+ Antiporter of Arabidopsis thaliana, Stimulates the Transport Activity.
M. Kawachi, Y. Kobae, T. Mimura, and M. Maeshima (2008)
J. Biol. Chem. 283, 8374-8383
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)