Law Alan W L, Lescar Julien, Hao Quan, Kotaka Masayo
Department of Physiology, Li Ka Shing Faculty of Medicine, University of Hong Kong, Hong Kong.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):671-4. doi: 10.1107/S1744309112015862. Epub 2012 May 23.
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 P3(1)21 or P3(2)21, with unit-cell parameters a = b = 123.49, c = 180.82 Å, α = β = 90, γ = 120°.
腺苷酸激酶（AKs）是一种磷酸转移酶，可催化腺嘌呤核苷酸的相互转化，从而在能量代谢中发挥重要作用。在恶性疟原虫中，已鉴定出三种AK同工型，即PfAK1、PfAK2和GTP:AMP磷酸转移酶（PfGAK）。PfAK1和PfAK2催化ATP和AMP转化为两分子ADP，而PfGAK对GTP和AMP表现出底物偏好，不接受ATP作为底物。PfGAK在大肠杆菌中克隆并表达，通过两步色谱法进行纯化。获得了PfGAK的棕色六方晶体，并进行了初步衍射分析。对单个PfGAK晶体的X射线衍射数据在空间群P3(1)21或P3(2)21中处理至2.9 Å分辨率，晶胞参数a = b = 123.49，c = 180.82 Å，α = β = 90，γ = 120°。
