Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli

JBIC Journal of Biological Inorganic Chemistry - Tập 13 - Trang 271-288 - 2007
Liliya A. Yatsunyk1, J. Allen Easton2, Lydia R. Kim1, Stacy A. Sugarbaker2, Brian Bennett3, Robert M. Breece4, Ivan I. Vorontsov5, David L. Tierney4, Michael W. Crowder2, Amy C. Rosenzweig1
1Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry, Northwestern University, Evanston, USA
2Department of Chemistry and Biochemistry, Miami University, Oxford, USA
3National Biomedical EPR Center, Department of Biophysics, Medical College of Wisconsin, Milwaukee, USA
4Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, USA
5Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Feinberg School of Medicine, Chicago, USA

Tóm tắt

ZnuA is the periplasmic Zn2+-binding protein associated with the high-affinity ATP-binding cassette ZnuABC transporter from Escherichia coli. Although several structures of ZnuA and its homologs have been determined, details regarding metal ion stoichiometry, affinity, and specificity as well as the mechanism of metal uptake and transfer remain unclear. The crystal structures of E. coli ZnuA (Eco-ZnuA) in the apo, Zn2+-bound, and Co2+-bound forms have been determined. ZnZnuA binds at least two metal ions. The first, observed previously in other structures, is coordinated tetrahedrally by Glu59, His60, His143, and His207. Replacement of Zn2+ with Co2+ results in almost identical coordination geometry at this site. The second metal binding site involves His224 and several yet to be identified residues from the His-rich loop that is unique to Zn2+ periplasmic metal binding receptors. Electron paramagnetic resonance and X-ray absorption spectroscopic data on CoZnuA provide additional insight into possible residues involved in this second site. The second site is also detected by metal analysis and circular dichroism (CD) titrations. Eco-ZnuA binds Zn2+ (estimated K d < 20 nM), Co2+, Ni2+, Cu2+, Cu+, and Cd2+, but not Mn2+. Finally, conformational changes upon metal binding observed in the crystal structures together with fluorescence and CD data indicate that only Zn2+ substantially stabilizes ZnuA and might facilitate recognition of ZnuB and subsequent metal transfer.

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JBIC Journal of Biological Inorganic Chemistry

Tập 13

271-288

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