Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe).

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-tRNA(Phe) after its purification by HPLC.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Nissen P,Reshetnikova L,Siboska G,Polekhina G,Thirup S,Kjeldgaard M,Clark BF,Nyborg J

doi

10.1016/0014-5793(94)01254-7

subject

Has Abstract

pub_date

1994-12-19 00:00:00

pages

165-8

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)01254-7

journal_volume

356

pub_type

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