Dr. Dax Fu
Biology Department
Brookhaven National Laboratory
Upton, NY

Monday, February 25, 2008
3:00 pm (CT)
3269 Beckman Institute

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. The x-ray structure of YiiP in complex with zinc has been recently solved at 3.8 Angstrom resolution (Science, 317, pp. 1746-1748, 2007) , showing that YiiP is a homodimer held together in a parallel orientation through four Zn2+ ions at the interface of the cytoplasmic domains 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. The lecture describes a higher resolution structure of Yiip recently obtained and discusses the mechanism of Yiip as deduced from structural and physiological studies.