Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe‐tRNAPhe

FEBS Letters

Clark, Brian F.C.¹  Nyborg, Jens¹  Nissen, Poul¹  Kjeldgaard, Morten¹  Thirup, Søren¹  Polekhina, Galina¹  Siboska, Gunhild¹  Reshetnikova, Ludmila² 

[1] Department of Biostructural Chemistry, Institute of Chemistry, University of Aarhus, Langelandsgade 140, DK-8000 Aarhus C, Denmark;Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov Str, 117984 Moscow, Russian Federation

关键词: Protein biosynthesis;    Elongation factor Tu;    Aminoacylated tRNA;    Ternary complex;    Crystallization;   

DOI  :  10.1016/0014-5793(94)01254-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Elongation factor Tu (EF-Tu) is the most abundant protein in prokaryotic cells. Its general function in protein biosynthesis is well established. It is a member of the large family of G-proteins, all of which bind guanosine phosphates (GDP or GTP) as cofactors. In its active GTP bound state EF-TU binds aminoacylated tRNA (aa-tRNA) forming the ternary complex EF-TU: GTP: aa-tRNA. The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA, GTPase activity is induced and inactive EF-TU: GDP is released. Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF-TU: GDPNP and yeast Phe-tRNA^phe after its purification by HPLC.

【 授权许可】

Unknown