2QFI

Structure of the zinc transporter YiiP

Summary for 2QFI

• Entry DOI: 10.2210/pdb2qfi/pdb
• Descriptor: Ferrous-iron efflux pump fieF, ZINC ION (2 entities in total)
• Functional Keywords: zinc transporter, transport protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P69380
• Total number of polymer chains: 2
• Total formula weight: 66372.19

Authors

Lu, M. (deposition date: 2007-06-27, release date: 2007-10-16, Last modification date: 2024-02-21)

Primary citation

Lu, M.,Fu, D.
Structure of the zinc transporter YiiP.
Science, 317:1746-1748, 2007

PubMed Abstract: 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.

PubMed: 17717154
DOI: 10.1126/science.1143748

Experimental method

X-RAY DIFFRACTION (3.8 Å)