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Abstract

Adenylate kinases (AKs) play important roles in nucleotide metabolism in all organisms and in cellular energetics by means of phosphotransfer networks in eukaryotes. The crystal structure of a human AK named AK6 was determined by in-house sulfur sing le-wavelength anomalous dispersion phasing methods and refined to 2.0-Angstrom resolution with a free R factor of 21.8%. Sequence analyses revealed that human AK6 belongs to a distinct subfamily of AKs present in all eukaryotic organisms sequenced so far. Enzymatic assays show that human AK6 has properties similar with other AKs, particularly with AK5. Fluorescence microscopy showed that human AK6 is localized predominantly to the nucleus of HeLa cells. The identification of a nuclear-localized AK sheds light on nucleotide metabolism in the nucleus and the energetic communication between mitochondria and nucleus by means of phosphotransfer networks.

Keywords

x-ray crystallography; nuclear localization; nucleoticle metabolism; phosphotransfer networks

Published in

Proceedings of the National Academy of Sciences
2005, volume: 102, number: 2, pages: 303-308
Publisher: NATL ACAD SCIENCES

SLU Authors

  • Wang, Liya

    • Department of Molecular Biosciences, Swedish University of Agricultural Sciences

  • Eriksson, Staffan

    • Department of Molecular Biosciences, Swedish University of Agricultural Sciences

Publication identifier

  • DOI: https://doi.org/10.1073/pnas.0407459102

Permanent link to this page (URI)

https://res.slu.se/id/publ/5691