Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe‐tRNAPhe
- 19 December 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 356 (2-3) , 165-168
- https://doi.org/10.1016/0014-5793(94)01254-7
Abstract
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-tRNAphe after its purification by HPLC.Keywords
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