2qfi
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(New page: 200px<br /><applet load="2qfi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qfi, resolution 3.80Å" /> '''Structure of the zin...)
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Revision as of 10:53, 23 January 2008
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Structure of the zinc transporter YiiP
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.
About this Structure
2QFI is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the zinc transporter YiiP., Lu M, Fu D, Science. 2007 Sep 21;317(5845):1746-8. Epub 2007 Aug 23. PMID:17717154
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