Structure of the zinc transporter YiiP

M Lu, D Fu - Science, 2007 - science.org
M Lu, D Fu
Science, 2007science.org
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 …
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.
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