Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95312
Title: Expression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferase
Authors: Law, Alan W. L.
Hao, Quan
Kotaka, Masayo
Lescar, Julien
Issue Date: 2012
Source: Law, A. W. L., Lescar, J., Hao, Q., & Kotaka, M. (2012). Expression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68(6), 671-674.
Series/Report no.: Acta Crystallographica Section F Structural Biology and Crystallization Communications
Abstract: Adenylate kinases (AKs) are phosphotransferase enzymes that catalyze the interconversion of adenine nucleotides, thereby playing an important role in energy metabolism. In Plasmodium falciparum, three AK isoforms, namely PfAK1, PfAK2 and GTP:AMP phosphotransferase (PfGAK), have been identified. While PfAK1 and PfAK2 catalyse the conversion of ATP and AMP to two molecules of ADP, PfGAK exhibits a substrate preference for GTP and AMP and does not accept ATP as a substrate. PfGAK was cloned and expressed in Escherichia coli and purified using two-step chromatography. Brown hexagonal crystals of PfGAK were obtained and a preliminary diffraction analysis was performed. X-ray diffraction data for a single PfGAK crystal were processed to 2.9 Å resolution in space group P3121 or P3221, with unit-cell parameters a = b = 123.49, c = 180.82 Å, α = β = 90, γ = 120°.
URI: https://hdl.handle.net/10356/95312
http://hdl.handle.net/10220/9157
ISSN: 1744-3091
DOI: http://dx.doi.org/10.1107/S1744309112015862
Rights: © 2012 International Union of Crystallography. This paper was published in Acta Crystallographica Section F Structural Biology and Crystallization Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [http://dx.doi.org/10.1107/S1744309112015862]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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