恶性疟原虫（PfPdxK）中吡哆醛激酶的纯化、结晶及初步X射线衍射分析
Purification, crystallization and preliminary X-ray diffraction analysis of pyridoxal kinase from Plasmodium falciparum (PfPdxK).
作者信息
Kronenberger Thales, Lunev Sergey, Wrenger Carsten, Groves Matthew R
机构信息
Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Sciences, University of Saõ Paulo, Avenida Professor Lineu Prestes 1374, Saõ Paulo-SP 05508-000, Brazil.
Department of Drug Design, Groningen Research Institute of Pharmacy (GRIP), Rijksuniversiteit Groningen (RUG), Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
出版信息
Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1550-5. doi: 10.1107/S2053230X14019864. Epub 2014 Oct 25.
Pyridoxal kinases (PdxK) catalyze the phosphorylation of vitamin B6 precursors. Thus, these enzymes are an essential part of many metabolic processes in all organisms. The protozoan parasite Plasmodium falciparum (the main causative agent of Malaria tropica) possesses a unique de novo B6-biosynthesis pathway in addition to a interconversion pathway based on the activity of plasmodial PdxK (PfPdxK). The role of PdxK in B6 salvage has prompted previous authors to suggest PdxK as a promising target for structure-based antimalarial drug design. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis of PfPdxK are reported. PfPdxK crystals have been grown in space group P2₁, with unit-cell parameters a=52.7, b=62.0, c=93.7 Å, β=95°. A data set has been collected to 2 Å resolution and an initial molecular-replacement solution is described.
吡哆醛激酶（PdxK）催化维生素B6前体的磷酸化。因此，这些酶是所有生物体中许多代谢过程的重要组成部分。原生动物寄生虫恶性疟原虫（热带疟疾的主要病原体）除了具有基于疟原虫PdxK（PfPdxK）活性的相互转化途径外，还拥有独特的从头合成B6的途径。PdxK在B6补救途径中的作用促使之前的作者提出将PdxK作为基于结构的抗疟药物设计的一个有前景的靶点。在此，报道了PfPdxK的表达、纯化、结晶及初步X射线衍射分析。PfPdxK晶体在空间群P2₁中生长，晶胞参数为a = 52.7、b = 62.0、c = 93.7 Å，β = 95°。已收集到分辨率为2 Å的数据集，并描述了初始分子置换解决方案。
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