Journal article

The crystal structures of a copper-bound metallochaperone from Saccharomyces cerevisiae

Mihwa Lee, N Dinesha G Cooray, Megan J Maher

Journal of Inorganic Biochemistry | ELSEVIER SCIENCE INC | Published : 2017


Atx1 is a metallochaperone protein from the yeast Saccharomyces cerevisiae (yAtx1) that plays a major role in copper homeostasis in this organism. yAtx1 functions as a copper transfer protein by shuttling copper to the secretory pathway to control intracellular copper levels. Here we describe the first crystal structures of yAtx1 that have been determined in the presence of Cu(I). The structures from two different crystal forms have been solved and refined to resolutions of 1.65 and 1.93Å. In contrast to the previous metallated crystal structure of yAtx1 where a single Hg(II) atom was coordinated by one yAtx1 molecule, the Cu(I)-yAtx1 was crystallised as a dimer in both crystal forms, sharin..

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University of Melbourne Researchers


Awarded by ARC

Awarded by ARC DECRA Fellowship

Funding Acknowledgements

This study was supported by the ARC grant DP140102746 to MJM and ARC DECRA Fellowship DE150101243 to ML. Aspects of this research were undertaken on the Macromolecular Crystallography beamline MX2 at the Australian Synchrotron (Victoria, Australia) and we thank the beamline staff for their enthusiastic and professional support. We acknowledge the kind gift of the pET11d-yAtx1 plasmid from Dr. Z. Xiao and Prof. Anthony Wedd (Bio21 Institute, University of Melbourne, Australia). We also acknowledge the La Trobe University Comprehensive Proteomics Platform for providing infrastructure.