2. Academic Validation
  3. The crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus

The crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus

  • Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):303-8. doi: 10.1073/pnas.0407459102.
Hui Ren 1,  Liya Wang,  Matthew Bennett,  Yuhe Liang,  Xiaofeng Zheng,  Fei Lu,  Lanfen Li,  Jie Nan,  Ming Luo,  Staffan Eriksson,  Chuanmao Zhang,  Xiao-Dong Su
Affiliations

Affiliation

  • 1 National Laboratory of Protein Engineering and Plant Genetic Engineering and Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing 100871, China.
PMID: 15630091 DOI: 10.1073/pnas.0407459102
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 single-wavelength anomalous dispersion phasing methods and refined to 2.0-A 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.

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