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

Hui Ren; Liya Wang; Matthew Bennett; Yuhe Liang; Xiaofeng Zheng; Fei Lu; Lanfen Li; Jie Nan; Ming Luo; Staffan Eriksson; Chuanmao Zhang; Xiao-Dong Su

doi:10.1073/pnas.0407459102

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

Hui Ren, Liya Wang, Matthew Bennett, Yuhe Liang, Xiaofeng Zheng, Fei Lu, Lanfen Li, Jie Nan, Ming Luo, Staffan Eriksson, Chuanmao Zhang, Xiao-Dong Su

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	303-8
Number of pages	6
Journal	Proceedings of the National Academy of Sciences
Volume	102
Issue number	2
DOIs	https://doi.org/10.1073/pnas.0407459102
Publication status	Published - 2005 Jan 11

Free keywords

Active Transport, Cell Nucleus
Adenylate Kinase
Amino Acid Sequence
Crystallography, X-Ray
HeLa Cells
Humans
Isoenzymes
Molecular Sequence Data
Nucleotides

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10.1073/pnas.0407459102

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title = "The crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus",

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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author = "Hui Ren and Liya Wang and Matthew Bennett and Yuhe Liang and Xiaofeng Zheng and Fei Lu and Lanfen Li and Jie Nan and Ming Luo and Staffan Eriksson and Chuanmao Zhang and Xiao-Dong Su",

year = "2005",

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doi = "10.1073/pnas.0407459102",

language = "English",

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journal = "Proceedings of the National Academy of Sciences",

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T1 - The crystal structure of human adenylate kinase 6

T2 - An adenylate kinase localized to the cell nucleus

AU - Ren, Hui

AU - Wang, Liya

AU - Bennett, Matthew

AU - Liang, Yuhe

AU - Zheng, Xiaofeng

AU - Lu, Fei

AU - Li, Lanfen

AU - Nan, Jie

AU - Luo, Ming

AU - Eriksson, Staffan

AU - Zhang, Chuanmao

AU - Su, Xiao-Dong

PY - 2005/1/11

Y1 - 2005/1/11

N2 - 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.

AB - 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.

KW - Active Transport, Cell Nucleus

KW - Adenylate Kinase

KW - Amino Acid Sequence

KW - Crystallography, X-Ray

KW - HeLa Cells

KW - Humans

KW - Isoenzymes

KW - Molecular Sequence Data

KW - Nucleotides

U2 - 10.1073/pnas.0407459102

DO - 10.1073/pnas.0407459102

M3 - Article

C2 - 15630091

SN - 0027-8424

VL - 102

SP - 303

EP - 308

JO - Proceedings of the National Academy of Sciences

JF - Proceedings of the National Academy of Sciences

IS - 2

ER -

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

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