2qfi
From Proteopedia
Structure of the zinc transporter YiiP
Structural highlights
Function[FIEF_ECOLI] Iron-efflux transporter responsible for iron detoxification. Also able to transport Zn(2+) in a proton-dependent manner.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYiiP 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. Structure of the zinc transporter YiiP.,Lu M, Fu D Science. 2007 Sep 21;317(5845):1746-8. Epub 2007 Aug 23. PMID:17717154[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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