2QFI: Structure Of The Zinc Transporter Yiip

Citation:
Science (2007) 317 p.1746-1748
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.
PDB ID: 2QFIDownload
MMDB ID: 59455
PDB Deposition Date: 2007/6/27
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 3.8  Å
Source Organism:
Similar Structures:
Biological Unit for 2QFI: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2QFI
Label Count Molecule
Proteins (2 molecules)
2
Ferrous-iron Efflux Pump Fief(Gene symbol: fieF)
Molecule annotation
Chemicals (4 molecules)
1
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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