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Sci. STKE, 25 September 2007
Vol. 2007, Issue 405, p. tw346
[DOI: 10.1126/stke.4052007tw346]

EDITORS' CHOICE

Structural Biology Transporting Zinc

Gilbert Chin

Science, AAAS, Washington, DC 20005, USA

The divalent zinc cation is found in multiple guises in prokaryotic and eukaryotic cells. Lu and Fu (see the Perspective by Nies) present the 3.8 angstrom structure of YiiP, a bacterial membrane protein that imports Zn2+ by exchanging it for H+. The structure of YiiP is a Y-shaped homodimer, through which a presumptive pathway for Zn2+/H+ exchange can be discerned. YiiP is a member of the cation diffusion facilitator family of transport proteins. Another family member, ZnT-8, is expressed solely in pancreatic beta cells and has recently been associated with risk for type 2 diabetes.

M. Lu, D. Fu, Structure of the zinc transporter YiiP. Science 317, 1746-1748 (2007). [Abstract] [Full Text]

D. H. Nies, How cells control zinc homeostasis. Science 317, 1695-1696 (2007). [Summary] [Full Text]

Citation: G. Chin, Transporting Zinc. Sci. STKE 2007, tw346 (2007).

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