Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

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
Prev | Table of Contents | Next

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

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Identification of the Zn2+ Binding Site and Mode of Operation of a Mammalian Zn2+ Transporter.
E. Ohana, E. Hoch, C. Keasar, T. Kambe, O. Yifrach, M. Hershfinkel, and I. Sekler (2009)
J. Biol. Chem. 284, 17677-17686
   Abstract »    Full Text »    PDF »
Copper Transport Activity of Yeast Ctr1 Is Down-regulated via Its C Terminus in Response to Excess Copper.
X. Wu, D. Sinani, H. Kim, and J. Lee (2009)
J. Biol. Chem. 284, 4112-4122
   Abstract »    Full Text »    PDF »
A Single Amino Acid Change in the Yeast Vacuolar Metal Transporters Zrc1 and Cot1 Alters Their Substrate Specificity.
H. Lin, A. Kumanovics, J. M. Nelson, D. E. Warner, D. M. Ward, and J. Kaplan (2008)
J. Biol. Chem. 283, 33865-33873
   Abstract »    Full Text »    PDF »
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 »


To Advertise     Find Products

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