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

Ren, Hui; Wang, Liya; Bennett, Matthew LU ; Liang, Yuhe; Zheng, Xiaofeng; Lu, Fei; Li, Lanfen; Nan, Jie LU ; Luo, Ming and Eriksson, Staffan LU , et al. (2005) In Proceedings of the National Academy of Sciences 102(2). p.8-303
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... (More)

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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publication status
published
keywords
Active Transport, Cell Nucleus, Adenylate Kinase, Amino Acid Sequence, Crystallography, X-Ray, HeLa Cells, Humans, Isoenzymes, Molecular Sequence Data, Nucleotides
in
Proceedings of the National Academy of Sciences
volume
102
issue
2
pages
6 pages
publisher
National Acad Sciences
external identifiers
  • scopus:19944428454
ISSN
0027-8424
DOI
10.1073/pnas.0407459102
language
English
LU publication?
yes
id
6812bcff-a586-47c8-8aef-3447be69bd12
date added to LUP
2016-09-07 22:54:42
date last changed
2017-07-02 04:53:53
@article{6812bcff-a586-47c8-8aef-3447be69bd12,
  abstract     = {<p>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.</p>},
  author       = {Ren, Hui and Wang, Liya and Bennett, Matthew and Liang, Yuhe and Zheng, Xiaofeng and Lu, Fei and Li, Lanfen and Nan, Jie and Luo, Ming and Eriksson, Staffan and Zhang, Chuanmao and Su, Xiao-Dong},
  issn         = {0027-8424},
  keyword      = {Active Transport, Cell Nucleus,Adenylate Kinase,Amino Acid Sequence,Crystallography, X-Ray,HeLa Cells,Humans,Isoenzymes,Molecular Sequence Data,Nucleotides},
  language     = {eng},
  month        = {01},
  number       = {2},
  pages        = {8--303},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {The crystal structure of human adenylate kinase 6 : An adenylate kinase localized to the cell nucleus},
  url          = {http://dx.doi.org/10.1073/pnas.0407459102},
  volume       = {102},
  year         = {2005},
}