2qfi: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: zinc transporter]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:57 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 18: / Line 18: @@
 [[Category: zinc transporter]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:53:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:57 2008''